Source: http://news.feedzilla.com/en_us/stories/politics/top-stories/309374106?client_source=feed&format=rss
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Friday, 31 May 2013
Radiation Makes a Manned Trip to Mars Impossible with Current Tech
Though Curiosity the rover can explore and see Mars up close, curious men and women of Earth will have to wait a bit longer. NASA reports that a manned trip to Mars is likely impossible with current technology because of radiation.
Curiosity's Radiation Assessment Detector (RAD) was able to measure the radiation of Mars from inside the spacecraft and found data that makes NASA reconsider the effectiveness of current radiation shielding. Specifically:
The findings, which are published in the May 31 edition of the journal Science, indicate radiation exposure for human explorers could exceed NASA's career limit for astronauts if current propulsion systems are used.
Two forms of radiation pose potential health risks to astronauts in deep space. One is galactic cosmic rays (GCRs), particles caused by supernova explosions and other high-energy events outside the solar system. The other is solar energetic particles (SEPs) associated with solar flares and coronal mass ejections from the sun.
Right now, spacecrafts do a better job at shielding against SEPs than they do GCRs. GCRs are highly energetic and penetrate the shielding on current spacecrafts. In order to protect astronauts from being exposed to radiation, NASA might have to invent better shielding. Or invent better something.
Exposure to radiation, which is measured in units of Sievert (Sv), increases the risk of cancer. We know that. Exposure to 1 Sv over time is associated with a five percent increase in risk of developing cancer. NASA's acceptable limit for its astronauts is a three percent increase in risk. Curiosity's RAD instruments measured an average of 1.8milliSv per day on its trip to Mars. The accumulated dose of the trip, according to Cary Zeitlin, lead paper in the findings and a principal scientist at the Southwest Research Institute (SwRI) in San Antonio, would be equivalent to "getting a whole-body CT scan once every five or six days". Yeah, that's too much.
But knowing this doesn't prevent a manned trip to Mars from ever happening. Knowing this helps protect the men and women who will take that manned trip to Mars. [NASA]
Source: http://gizmodo.com/radiation-makes-a-manned-trip-to-mars-impossible-with-c-510606694
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Thursday, 30 May 2013
Calculated Risk: MBA: Mortgage Purchase Applications increase ...
by Bill McBride on 5/29/2013 09:14:00 AM
From the MBA: Mortgage Applications Decrease in Latest MBA Weekly Survey
The Refinance Index decreased 12 percent, the largest single week drop in refinance applications this year, from the previous week to the lowest level since December 2012. The seasonally adjusted Purchase Index increased 3 percent from one week earlier.
...
"Refinance applications fell for the third straight week bringing the refinance index to its lowest level since December 2012 as mortgage rates increased to their highest level in a year,? said Mike Fratantoni, MBA?s Vice President of Research and Economics. ?Rates rose in response to stronger economic data and an increasing chance that the Fed may soon begin to taper their asset purchases."The average contract interest rate for 30-year fixed-rate mortgages with conforming loan balances ($417,500 or less) increased to 3.90 percent, the highest rate since May 2012, from 3.78 percent, with points unchanged at 0.39 (including the origination fee) for 80 percent loan-to-value ratio (LTV) loans.
emphasis added
Click on graph for larger image.The first graph shows the refinance index.
There?has been a sustained refinance boom for over a year.
However the index is down almost 30% over the last three weeks, and this is the lowest level since last December.
The second graph shows the MBA mortgage purchase index.? The 4-week average of the purchase index has generally been trending up?over the last year, and the?4-week average of the?purchase index is up about 10% from a year ago.
Source: http://www.calculatedriskblog.com/2013/05/mba-mortgage-purchase-applications.html
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How computers can learn better - R&D Magazine
Reinforcement learning is a technique, common in computer science, in which a computer system learns how best to solve some problem through trial-and-error. Classic applications of reinforcement learning involve problems as diverse as robot navigation, network administration, and automated surveillance.
At the Association for Uncertainty in Artificial Intelligence?s annual conference this summer (2013), researchers from Massachusetts Institute of Technology (MIT)?s Laboratory for Information and Decision Systems (LIDS) and Computer Science and Artificial Intelligence Laboratory will present a new reinforcement-learning algorithm that, for a wide range of problems, allows computer systems to find solutions much more efficiently than previous algorithms did.
The paper also represents the first application of a new programming framework that the researchers developed, which makes it much easier to set up and run reinforcement-learning experiments. Alborz Geramifard, a LIDS postdoctoral researcher and first author of the new paper, hopes that the software, dubbed RLPy (for reinforcement learning and Python, the programming language it uses), will allow researchers to more efficiently test new algorithms and compare algorithms? performance on different tasks. It could also be a useful tool for teaching computer-science students about the principles of reinforcement learning.
Geramifard developed RLPy with Robert Klein, a master?s student in MIT?s Dept. of Aeronautics and Astronautics. RLPy and its source code were both released online in April (2013).
Every reinforcement-learning experiment involves what?s called an agent, which in artificial-intelligence research is often a computer system being trained to perform some task. The agent might be a robot learning to navigate its environment, or a software agent learning how to automatically manage a computer network. The agent has reliable information about the current state of some system: The robot might know where it is in a room, while the network administrator might know which computers in the network are operational and which have shut down. But there?s some information the agent is missing?what obstacles the room contains, for instance, or how computational tasks are divided up among the computers.
Finally, the experiment involves a ?reward function,? a quantitative measure of the progress the agent is making on its task. That measure could be positive or negative: The network administrator, for instance, could be rewarded for every failed computer it gets up and running but penalized for every computer that goes down.
The goal of the experiment is for the agent to learn a set of policies that will maximize its reward, given any state of the system. Part of that process is to evaluate each new policy over as many states as possible. But exhaustively canvassing all of the system?s states could be prohibitively time-consuming.
Consider, for instance, the network-administration problem. Suppose that the administrator has observed that in several cases, rebooting just a few computers restored the whole network. Is that a generally applicable solution?
One way to answer that question would be to evaluate every possible failure state of the network. But even for a network of only 20 machines, each of which has only two possible states?working or not?that would mean canvassing a million possibilities.
Faced with such a combinatorial explosion, a standard approach in reinforcement learning is to try to identify a set of system ?features? that approximate a much larger number of states. For instance, it might turn out that when computers 12 and 17 are down, it rarely matters how many other computers have failed: A particular reboot policy will almost always work. The failure of 12 and 17 thus stands in for the failure of 12, 17, and 1; of 12, 17, 1, and 2; of 12, 17, and 2, and so on.
Geramifard?along with Jonathan How, the Richard Cockburn Maclaurin Professor of Aeronautics and Astronautics, Thomas Walsh, a postdoctoral researcher in How?s laboratory, and Nicholas Roy, an associate professor of aeronautics and astronautics?developed a new technique for identifying pertinent features in reinforcement-learning tasks. The algorithm first builds a data structure known as a tree?kind of like a family-tree diagram?that represents different combinations of features. In the case of the network problem, the top layer of the tree would be individual machines, the next layer would be combinations of two machines, the third layer would be combinations of three machines, and so on.
The algorithm then begins investigating the tree, determining which combinations of features dictate a policy?s success or failure. The relatively simple key to its efficiency is that when it notices that certain combinations consistently yield the same outcome, it stops exploring them. For instance, if it notices that same policy seems to work whenever machines 12 and 17 have failed, it stops considering combinations that include 12 and 17 and begins looking for others.
Geramifard believes that this approach captures something about how human beings learn to perform new tasks. ?If you teach a small child what a horse is, at first it might think that everything with four legs is a horse,? he says. ?But when you show it a cow, it learns to look for a different feature?say, horns.? In the same way, Geramifard explains, the new algorithm identifies an initial feature on which to base judgments and then looks for complementary features that can refine the initial judgment.
RLPy allowed the researchers to quickly test their new algorithm against a number of others. ?Think of it as like a Lego set,? Geramifard says. ?You can snap one module out and snap another one in its place.?
In particular, RLPy comes with a number of standard modules that represent different machine-learning algorithms; different problems (such as the network-administration problem, some standard control-theory problems that involve balancing pendulums, and some standard surveillance problems); different techniques for modeling the computer system?s environment; and different types of agents.
It also allows anyone familiar with the Python programming language to build new modules. They just have to be able to hook up with existing modules in prescribed ways.
Geramifard and his colleagues found that in computer simulations, their new algorithm evaluated policies more efficiently than its predecessors, arriving at more reliable predictions in one-fifth the time.
RLPy can be used to set up experiments that involve computer simulations, such as those that the MIT researchers evaluated, but it can also be used to set up experiments that collect data from real-world interactions. In one ongoing project, for instance, Geramifard and his colleagues plan to use RLPy to run an experiment involving an autonomous vehicle learning to navigate its environment. In the project?s initial stages, however, he?s using simulations to begin building a battery of reasonably good policies. ?While it?s learning, you don?t want to run it into a wall and wreck your equipment,? he says.
Source: Massachusetts Institute of Technology
Source: http://www.rdmag.com/news/2013/05/how-computers-can-learn-better
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Samsung Galaxy Exhibit available today on T-Mobile for $19.99 down
T-Mobile this morning announced that the Samsung Galaxy Exhibit is now available online and in select stores. The decidedly entry-level device runs $19 down with 24 monthly payments of $9, or $235 outright. For your trouble you get Android 4.1.2 Jelly Bean, a 5-megapixel camera, a 4-inch WVGA display, and a mere 1,500 mAh battery.
If you're looking for your first smartphone, chances are you'll get steered toward this. which essentially is a Samsung Galaxy S3 Mini. Just know you're starting at the low end, and work your way up from there.
More: T-Mobile
     |
Source: http://feedproxy.google.com/~r/androidcentral/~3/7a14VUcAw6g/story01.htm
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Review: Toshiba KIRABook 13 i7 Touch
Source: http://feedproxy.google.com/~r/GearFactor/~3/kxi2kO7FMF0/
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Duke celebrates 2nd NCAA lacrosse title
WRALSportsFan
Duke celebrates 2nd NCAA lacrosse title
Published: 2013-05-28 15:51:00
Updated: 2013-05-28 19:25:14
Yesterday at 7:25 p.m.
DURHAM, N.C. ? Duke celebrated its latest national championship in lacrosse like it had already won one before.
Which makes sense, because some of the Blue Devils already had.
So after Duke beat Syracuse to win its second NCAA title in four years, coach John Danowski had his players remove their championship caps and T-shirts, tone down the party and shake the Orange players' hands with grace and humility.
Danowski said Tuesday that "it just never made sense to me to put on a T-shirt that said, 'We beat you'" because "it doesn't seem to be sportsmanlike."
These Blue Devils let their results on the field speak for themselves.
Duke is the only program in Division I to reach each of the last seven Final Fours.
The Blue Devils have made it that far every year since Danowski took over the program in the summer of 2006, and the high point in that run came in 2010 when they won their first national title.
And during the past four years, the freshmen on that team developed into the seniors who delivered a second championship ? a 16-10 victory over the Orange after they fell behind 5-0 and appeared headed for their second title-game loss under Danowski.
The win made Danowski the fifth active coach in Division I with multiple national titles.
"I think it proves to everybody that what we do here is right," junior attacker Josh Dionne said. "What coach Danowski preaches to us, the discipline, he makes us mature very quickly. The greatness that he demands of us, that's a bar set so high."
Few expected a second title early in the season, when the Blue Devils lost four of their first six games ? including a 16-7 loss to Maryland that came a day after Danowski threw the team off the practice field because the players were lacking energy and sharpness.
"That was the last time that looked like that the day before a game," Danowski said. "One of the lessons that this team had to learn."
By season's end, Duke hardly resembled the team that stumbled out of the gate. The Blue Devils won 14 of their final 15 games, with the only loss coming to rival North Carolina in the ACC championship game.
Duke won its first three NCAA tournament games by a combined four goals, then came up with a timely rally to beat the Orange on Monday and claim another championship trophy.
This one came with a more mellow celebration, after Danowski's request to his team was unknowingly captured by television cameras.
"It just shows everyone who's watching what kind of person coach Danowski is," Dionne said. "It just shows that he is a winner. He knows the values and he's been there and lost so many times that he knows how the other coach feels."
It also marked the latest step forward from the infamous, since-debunked rape case that was brought in 2006 against three players and led to Danowski being hired that summer to replace former coach Mike Pressler.
"I can't help but think we've come full circle here in some ways," Danowski said. "Never in my wildest dreams did I think we'd be sitting here. You don't think in terms of wins and losses and championships and sitting here next to the trophy."
___
Follow Joedy McCreary on Twitter at (at)JoedyAP.
Copyright 2013 by The Associated Press. All rights reserved. This material may not be published, broadcast, rewritten or redistributed.
Most Recent Comments
RE: Duke celebrates 2nd NCAA lacrosse title
Just gotten into lacrosse the last few years. Happy to see an exciting sport grow & give an alternative to a painfully boring sport like baseball?
- Posted by canz
Agreed. It is also nice to see that the local ACC schools - both men and women - are doing well in what has traditionally been a "northern school" sport.
I would like to say, however, being at a local minor league baseball game in person is much more fun than watching on TV. The Durham Bulls put on a great show. Take the family and check them out.
RE: Duke celebrates 2nd NCAA lacrosse title
Just gotten into lacrosse the last few years. Happy to see an exciting sport grow & give an alternative to a painfully boring sport like baseballRE: Duke celebrates 2nd NCAA lacrosse title
Way to go guys, I have to admit when it was 5-0 I was very concerned.You guys showed great heart battling back in bringing the championship
back to Durham!
RE: Duke celebrates 2nd NCAA lacrosse title
Congrats guys!Source: http://www.wralsportsfan.com/duke-celebrates-2nd-ncaa-lacrosse-title/12491530/
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Tuesday, 28 May 2013
Global money laundering operation busted
By Emily Flitter
NEW YORK (Reuters) - U.S. prosecutors have indicted the operators of digital currency exchange Liberty Reserve, accusing the Costa Rica-based company of helping criminals around the world launder more than $6 billion in illicit funds linked to everything from child pornography to software for hacking into banks.
The indictment unsealed on Tuesday said Liberty Reserve had more than a million users worldwide, including at least 200,000 in the United States, and virtually all of its business was related to suspected criminal activity.
"Liberty Reserve has emerged as one of the principal means by which cyber-criminals around the world distribute, store and launder the proceeds of their illegal activity," according to the indictment filed in U.S. District Court for the Southern District of New York.
Officials said authorities in Spain, Costa Rica and New York arrested five people on Friday, including the company's founder, Arthur Budovsky, and seized bank accounts and Internet domains associated with Liberty Reserve.
Digital currency is made up of transferable units that can be exchanged for cash. Over the past decade, its use has expanded, attracting attention from the media and Wall Street. The most widely known digital currency is called Bitcoin. Liberty Reserve's currency was not connected to Bitcoin.
The indictment detailed a system of payments that allowed users to open accounts with little information and move money around with anonymity.
The U.S. Treasury named Liberty Reserve under the USA Patriot Act as a company "specifically designed and frequently used to facilitate money laundering in cyber space."
That designation, the first against a virtual currency exchange, prohibits banks or other payment processors from doing any business with Liberty Reserve, even if it should reopen under a new name.
In addition to pornography and drug trafficking funds, Liberty Reserve's virtual currency was also used to anonymously buy and sell software designed to steal personal information, according to a statement from the U.S. Treasury.
Users could also buy malware programs designed to assault financial institutions, as well as lists of information from thousands of compromised personal accounts, the Treasury said.
In addition to Budovsky, his deputy, Azzedine El Amine was arrested, as was co-founder Vladimir Kats, and two technology designers, Maxim Chukarev and Mark Marmilev.
Two more company employees were still at large in Costa Rica according to officials: Ahmed Yassine Abdelghani and Allan Esteban Hidalgo Jimenez. According to the indictment, almost all of the men used the alias, Eric Paltz.
None of the men could be reached for comment.
According to the indictment, Liberty Reserve's currency unit was called the "LR." Users opened accounts at Liberty Reserve giving only a name, address and date of birth that the company made no attempt to verify.
Once a user had a Liberty Reserve account, he or she could use cash to purchase LRs from third-party exchange merchants, which traded LRs with each other in bulk and charged fees to make the exchanges between LRs and hard cash.
Liberty Reserve users could transfer the digital currency units called LRs to each other, to be redeemed in different parts of the world for cash using the third-party exchange companies.
The third party exchange companies provided the gateway to more conventional payment systems. According to information Liberty Reserve's archived web pages, the company had relationships at one time with at least 35 different exchange companies, some of which transferred cash back and forth to customers using PayPal, Western Union, MoneyGram, credit cards including Visa, Mastercard, American Express, and CitiBank Global Money Transfer.
The indictment said Liberty Reserve did not collect any banking or transaction information from the third-party exchange companies. It also let its users hide their Liberty Exchange account numbers when making transactions, which offered another opportunity for the users to mask their true identities.
The company processed around 12 million financial transactions per year. Since it began operating in 2006, the indictment said, Liberty Reserve laundered over $6 billion in criminal proceeds.
On Tuesday, the company's website, www.libertyreserve.com, displayed the message: "This domain name has been seized by the United States Global Illicit Financial Team."
It was not clear whether the people arrested in Spain and Costa Rica would be extradited to the United States or when the two people arrested in Brooklyn, New York, would appear in court.
Regulatory obligations to combat money laundering have emerged as a major challenge to digital currency firms. The U.S. Treasury Department's anti-money laundering unit, the Financial Crimes Enforcement Network (FinCEN), issued guidance in March that labeled digital currency firms as money transmitters, thereby obliging them to enact anti-money laundering programs and register with FinCEN.
A top Bitcoin exchange, Tokyo-based Mt. Gox, failed to register with FinCEN earlier this month and had its U.S. dollar accounts seized by authorities.
Over the past week, a Bitcoin unit has traded at around $130, according to the website Bitcoincharts.com.
(Reporting by Emily Flitter in New York; Additional reporting by Brett Wolf in St. Louis and Isabella Cota Schwarz in San Jose, Costa Rica and Matthew Goldstein in New York; Editing by Jeffrey Benkoe, Tim Dobbyn and Jan Paschal)
Source: http://news.yahoo.com/u-shuts-alleged-cyber-criminal-money-transfer-system-144155238.html
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Hang Up and Listen: The Grappling with Sportocrats Edition
?Listen to "Hang Up and Listen" with Stefan Fatsis, Josh Levin, and Mike Pesca by clicking the arrow on the audio player below:
Hang Up and Listen is brought to you by?Stamps.com.?Click on the radio microphone and enter HANGUP to get our $110 bonus offer.
In this week?s episode of?Slate?s sports podcast Hang Up and Listen, Stefan Fatsis, Josh Levin, and Mike Pesca are joined by Irish soccer journalist Ken Early to discuss the Champions League and the retirements of David Beckham and Alex Ferguson. Bill Scherr, the head of the Committee for the Preservation of Olympic Wrestling, also joins to discuss the impending IOC vote on whether the sport will lose its spot in the Olympics. Finally, they assess whether the arrival of three new college stars can springboard the WNBA to new levels of popularity.
Here are links to some of the articles and other items mentioned on the show:
Hang Up and Listen?s weekly wizzers:
Podcast production and edit by Mike Vuolo. Our intern is Michael Gerber.
Source: http://feeds.slate.com/click.phdo?i=d7813217d3fa5c1908053fd4ced0db41
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Ifi is offering new jobs for artists at their portal
28 May 2013, Delhi, India: People who have real talent and passionate about Film and TV industry, or want to make their career in Glamour industry. Can register them self on IFI portal for getting artist jobs. IFI can be a great place for finding jobs in Films and Glamour industry.
Talking about the jobs available for the Artists, a senior promoter from International Film Industry states, people wanting job as artist may apply for jobs after registering on IFI website. People may apply for jobs listing in Delhi, Mumbai, and Bangalore, Chennai and all major cities and countries across the globe.
Applying for the Artist jobs through International Film Industry give you a great benefit in finding jobs and get selected quickly after registering. All others jobs related to film making are also available on website.
Speaking about the Artist Jobs, a senior official from IFI commented, complete details about the jobs available for artists are provided on our website, and helps in providing all the required information to users. Interested people can visit the website or can contact directly at our helpdesk number.
About International Film Industry
International Film Industry is an online multi beneficial platform, which not only gives opportunity to its user to apply for a job, but also provides a strong platform to advertise their business or services on the website. International Film Industry also offers various paid membership plan which provides extra features to its registered users.
Contact Information: For more information please contact ?
Corporate Office:
Plot No.4, Block-C, Community Centre,
Near Janak Cinema, Janakpuri, New Delhi-110058
Mobile No: 08860635775
Email: info@internationalfilmindustry.com
Website: http://www.internationalfilmindustry.com/
###
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Monday, 27 May 2013
Star-Crossed Cat Lovers: Tony The Cat Tries To Get To His Girlfriend (VIDEO)
"Be but sworn my love and I will no longer be a Cat-pulet..."
Via Tastefully Offensive
Also on HuffPost:
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Salmonella uses protective switch during infection
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Public release date: 27-May-2013[ | E-mail |
Share ] Contact: Mary Beckman
mary.beckman@pnnl.gov
509-375-3688
DOE/Pacific Northwest National Laboratory
Possibly energy-conserving, switch suggests metabolic changes that researchers might exploit to fight systemic illness
RICHLAND, Wash. -- For the first time, researchers have found a particular kind of molecular switch in the food poisoning bacteria Salmonella Typhimurium under infection-like conditions. This switch, using a process called S-thiolation, appears to be used by the bacteria to respond to changes in the environment during infection and might protect it from harm, researchers report this week online in the Proceedings of the National Academy of Sciences Early Edition.
S-thiolation protects proteins from irreversible chemical changes when a cell is stressed. The newly discovered switch might regulate when or how proteins work while offering protection, providing researchers insight into Salmonella infection.
"We continue to recognize just how clever this bug is in adapting to its environment," said systems biologist Josh Adkins of the Department of Energy's Pacific Northwest National Laboratory. "During infection it lives in hostile environments, and so it can use multiple approaches to adjust its functions."
Whole Ensemble
Salmonella Typhimurium causes food poisoning in people and can be fatal in the elderly or very young. Recent technological advances in the field known as proteomics are allowing researchers to explore how proteins, the workhorses of the cell, allow the bacteria to infect and cause illness. Most technologies that examine a cell's ensemble of proteins do so by chopping the proteins up. Adkins, lead author Charles Ansong and other colleagues wanted to look at whole proteins, which provides more information such as how proteins are regulated.
Cells regulate how proteins work in several ways. One of the most common adds molecular pieces that serve as gas pedals on proteins, turning them up or down in a grand orchestrated way. Proteomics methods that chop up proteins allow a researcher to determine that a particular protein was present, but not if it was actually functioning. Those methods also destroy evidence about how hard the gas pedal was pressed.
To identify which proteins were likely turned on or off during Salmonella infection, the team grew the bacteria either with rich food that satisfied all their nutritional needs or with nutrient-poor food that mimicked the kind of stressful environment the microbes find themselves in while infecting someone.
Then the researchers took samples of the bacteria and identified the proteins inside. They used a method called top-down proteomics, a technological advancement that allows researchers to look at wide swaths of whole proteins instead of just a few at a time. The team identified 563 unique proteins. This number is comparable to fungus and human studies but almost three times as many as in other bacterial studies using top-down proteomics.
They also determined if the proteins had molecular modifications on them. These can cap an end of a protein or dot the protein's length. Because different modifications can be mixed and matched on one protein, they ended up with a total of 1,665 different forms of the 563 unique proteins.
"This study shows how well top-down proteomics works, especially to get at regulatory information," said co-author Liljana Pasa-Tolic, who led top-down proteomics development with mass spectroscopist Si Wu at EMSL, DOE's Environmental Molecular Sciences Laboratory on the PNNL campus.
Gluts Versus Cysts
Of particular interest to the team were S-thiolation modifications. These modifications cover and protect a protein's sulfur atoms, which tend to snag each other like velcro and cause misshapen proteins. The modifications come in two flavors: a bulky glutathione and a compact cysteine. While glutathione modifications are pretty well studied, only four studies reveal cysteine modifications, and only two of those are in bacteria.
A total of 25 proteins sported glutathiones and another 18 wore cysteines. But nine of these stood out: The glutathiones and the cysteines attached to the same exact spot on the nine proteins. Not at the same time -- the team found that Salmonella used glutathiones at these sites when they were fat and happy, growing with rich food. When grown under stressful conditions with nutritionally poor food, the Salmonella swapped their glutathiones for cysteines.
In addition, switching S-thiolation modifications appeared to be a talent unique to Salmonella. The team checked other bacteria such as Escherichia coli, a common gut bacteria, and Yersinia pestis, which causes plague, to see if other species used this S-thiolation switch on their proteins. They didn't, suggesting that Salmonella had come up with this tactic during its own evolution.
The researchers speculate that Salmonella might use the smaller cysteine under stressed conditions as an energy saving device. Additional research will reveal what control functions the modifications are actually performing on the proteins.
###
This work was supported by the National Institute of Allergy and Infectious Disease through interagency agreement Y1-AI-8494-01 and the National Institute for General Medical Sciences.
Reference: Charles Ansong, Si Wu, Da Meng, Xiaowen Liu, Heather Brewer, Brooke L. Deatherage Kaiser, Ernesto S. Nakayasu, John R. Cort, Pavel A. Pevzner, Richard D. Smith, Fred Heffron, Joshua N. Adkins and Ljiljana Paa-Toli?. Top-down proteomics reveals a unique protein S-thiolation switch in Salmonella Typhimurium in response to infection-like conditions, Proc Natl Acad Sci U S A, Early Edition online the week of May 27, 2013, DOI 10.1073/pnas.1221210110.
EMSL, the Environmental Molecular Sciences Laboratory, is a national scientific user facility sponsored by the Department of Energy's Office of Science. Located at Pacific Northwest National Laboratory in Richland, Wash., EMSL offers an open, collaborative environment for scientific discovery to researchers around the world. Its integrated computational and experimental resources enable researchers to realize important scientific insights and create new technologies. Follow EMSL on Facebook, LinkedIn and Twitter.
Interdisciplinary teams at Pacific Northwest National Laboratory address many of America's most pressing issues in energy, the environment and national security through advances in basic and applied science. PNNL employs 4,500 staff, has an annual budget of nearly $1 billion, and has been managed for the U.S. Department of Energy by Ohio-based Battelle since the laboratory's inception in 1965. For more, visit the PNNL's News Center, or follow PNNL on Facebook, LinkedIn and Twitter.
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Public release date: 27-May-2013[ | E-mail |
Share ] Contact: Mary Beckman
mary.beckman@pnnl.gov
509-375-3688
DOE/Pacific Northwest National Laboratory
Possibly energy-conserving, switch suggests metabolic changes that researchers might exploit to fight systemic illness
RICHLAND, Wash. -- For the first time, researchers have found a particular kind of molecular switch in the food poisoning bacteria Salmonella Typhimurium under infection-like conditions. This switch, using a process called S-thiolation, appears to be used by the bacteria to respond to changes in the environment during infection and might protect it from harm, researchers report this week online in the Proceedings of the National Academy of Sciences Early Edition.
S-thiolation protects proteins from irreversible chemical changes when a cell is stressed. The newly discovered switch might regulate when or how proteins work while offering protection, providing researchers insight into Salmonella infection.
"We continue to recognize just how clever this bug is in adapting to its environment," said systems biologist Josh Adkins of the Department of Energy's Pacific Northwest National Laboratory. "During infection it lives in hostile environments, and so it can use multiple approaches to adjust its functions."
Whole Ensemble
Salmonella Typhimurium causes food poisoning in people and can be fatal in the elderly or very young. Recent technological advances in the field known as proteomics are allowing researchers to explore how proteins, the workhorses of the cell, allow the bacteria to infect and cause illness. Most technologies that examine a cell's ensemble of proteins do so by chopping the proteins up. Adkins, lead author Charles Ansong and other colleagues wanted to look at whole proteins, which provides more information such as how proteins are regulated.
Cells regulate how proteins work in several ways. One of the most common adds molecular pieces that serve as gas pedals on proteins, turning them up or down in a grand orchestrated way. Proteomics methods that chop up proteins allow a researcher to determine that a particular protein was present, but not if it was actually functioning. Those methods also destroy evidence about how hard the gas pedal was pressed.
To identify which proteins were likely turned on or off during Salmonella infection, the team grew the bacteria either with rich food that satisfied all their nutritional needs or with nutrient-poor food that mimicked the kind of stressful environment the microbes find themselves in while infecting someone.
Then the researchers took samples of the bacteria and identified the proteins inside. They used a method called top-down proteomics, a technological advancement that allows researchers to look at wide swaths of whole proteins instead of just a few at a time. The team identified 563 unique proteins. This number is comparable to fungus and human studies but almost three times as many as in other bacterial studies using top-down proteomics.
They also determined if the proteins had molecular modifications on them. These can cap an end of a protein or dot the protein's length. Because different modifications can be mixed and matched on one protein, they ended up with a total of 1,665 different forms of the 563 unique proteins.
"This study shows how well top-down proteomics works, especially to get at regulatory information," said co-author Liljana Pasa-Tolic, who led top-down proteomics development with mass spectroscopist Si Wu at EMSL, DOE's Environmental Molecular Sciences Laboratory on the PNNL campus.
Gluts Versus Cysts
Of particular interest to the team were S-thiolation modifications. These modifications cover and protect a protein's sulfur atoms, which tend to snag each other like velcro and cause misshapen proteins. The modifications come in two flavors: a bulky glutathione and a compact cysteine. While glutathione modifications are pretty well studied, only four studies reveal cysteine modifications, and only two of those are in bacteria.
A total of 25 proteins sported glutathiones and another 18 wore cysteines. But nine of these stood out: The glutathiones and the cysteines attached to the same exact spot on the nine proteins. Not at the same time -- the team found that Salmonella used glutathiones at these sites when they were fat and happy, growing with rich food. When grown under stressful conditions with nutritionally poor food, the Salmonella swapped their glutathiones for cysteines.
In addition, switching S-thiolation modifications appeared to be a talent unique to Salmonella. The team checked other bacteria such as Escherichia coli, a common gut bacteria, and Yersinia pestis, which causes plague, to see if other species used this S-thiolation switch on their proteins. They didn't, suggesting that Salmonella had come up with this tactic during its own evolution.
The researchers speculate that Salmonella might use the smaller cysteine under stressed conditions as an energy saving device. Additional research will reveal what control functions the modifications are actually performing on the proteins.
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This work was supported by the National Institute of Allergy and Infectious Disease through interagency agreement Y1-AI-8494-01 and the National Institute for General Medical Sciences.
Reference: Charles Ansong, Si Wu, Da Meng, Xiaowen Liu, Heather Brewer, Brooke L. Deatherage Kaiser, Ernesto S. Nakayasu, John R. Cort, Pavel A. Pevzner, Richard D. Smith, Fred Heffron, Joshua N. Adkins and Ljiljana Paa-Toli?. Top-down proteomics reveals a unique protein S-thiolation switch in Salmonella Typhimurium in response to infection-like conditions, Proc Natl Acad Sci U S A, Early Edition online the week of May 27, 2013, DOI 10.1073/pnas.1221210110.
EMSL, the Environmental Molecular Sciences Laboratory, is a national scientific user facility sponsored by the Department of Energy's Office of Science. Located at Pacific Northwest National Laboratory in Richland, Wash., EMSL offers an open, collaborative environment for scientific discovery to researchers around the world. Its integrated computational and experimental resources enable researchers to realize important scientific insights and create new technologies. Follow EMSL on Facebook, LinkedIn and Twitter.
Interdisciplinary teams at Pacific Northwest National Laboratory address many of America's most pressing issues in energy, the environment and national security through advances in basic and applied science. PNNL employs 4,500 staff, has an annual budget of nearly $1 billion, and has been managed for the U.S. Department of Energy by Ohio-based Battelle since the laboratory's inception in 1965. For more, visit the PNNL's News Center, or follow PNNL on Facebook, LinkedIn and Twitter.
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Source: http://www.eurekalert.org/pub_releases/2013-05/dnnl-sup052313.php
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