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* The precise functions of serine [[Protein kinases and phosphatases|protein kinases]] in ''B. subtilis'' have largely remained enigmatic until very recently. Now, two studies from the lab of [[Jonathan Dworkin]] describe functions and molecular targets for two of these kinases, [[PrkC]] and [[YabT]]. [http://www.ncbi.nlm.nih.gov/pubmed/26056311 Pereira et al.] have identified the universally conserved [[TufA|elongation factor Tu]] as a target for the protein kinase [[YabT]]. In srarving cells, YabT phosphorylates [[TufA|EF-Tu]] at a conserved threonine residue. Phosphorylation impairs the essential GTPase activity of [[TufA|EF-Tu]], thereby preventing its release from the [[ribosome]]. As a consequence, phosphorylated [[TufA|EF-Tu]] has a dominant-negative effect in [[translation]] elongation, resulting in the overall inhibition of protein synthesis. Importantly, this mechanism allows a quick and robust regulation of one of the [[most abundant proteins|most abundant cellular proteins]]. [http://www.ncbi.nlm.nih.gov/pubmed/26102633 Libby et al.] have uncovered that phosphorylation by PrkC stimulates the activity of the [[essential genes|essential]] [[Two-component systems|two-component transcription factor]] [[WalR]]. This mechanism links the presence of muropeptides that trigger [[PrkC]] activity to the expression of the genes of the [[WalR regulon]] that are involved in [[cell wall synthesis|cell wall metabolism]]. | * The precise functions of serine [[Protein kinases and phosphatases|protein kinases]] in ''B. subtilis'' have largely remained enigmatic until very recently. Now, two studies from the lab of [[Jonathan Dworkin]] describe functions and molecular targets for two of these kinases, [[PrkC]] and [[YabT]]. [http://www.ncbi.nlm.nih.gov/pubmed/26056311 Pereira et al.] have identified the universally conserved [[TufA|elongation factor Tu]] as a target for the protein kinase [[YabT]]. In srarving cells, YabT phosphorylates [[TufA|EF-Tu]] at a conserved threonine residue. Phosphorylation impairs the essential GTPase activity of [[TufA|EF-Tu]], thereby preventing its release from the [[ribosome]]. As a consequence, phosphorylated [[TufA|EF-Tu]] has a dominant-negative effect in [[translation]] elongation, resulting in the overall inhibition of protein synthesis. Importantly, this mechanism allows a quick and robust regulation of one of the [[most abundant proteins|most abundant cellular proteins]]. [http://www.ncbi.nlm.nih.gov/pubmed/26102633 Libby et al.] have uncovered that phosphorylation by PrkC stimulates the activity of the [[essential genes|essential]] [[Two-component systems|two-component transcription factor]] [[WalR]]. This mechanism links the presence of muropeptides that trigger [[PrkC]] activity to the expression of the genes of the [[WalR regulon]] that are involved in [[cell wall synthesis|cell wall metabolism]]. | ||
* '''Relevant ''Subti''Wiki pages:''' [[Jonathan Dworkin]], [[Protein kinases and phosphatases|protein kinases]], [[YabT]], [[TufA|EF-Tu]], [[PrkC]], [[WalR]], [[cell wall synthesis|cell wall metabolism]] | * '''Relevant ''Subti''Wiki pages:''' [[Jonathan Dworkin]], [[Protein kinases and phosphatases|protein kinases]], [[YabT]], [[TufA|EF-Tu]], [[PrkC]], [[WalR]], [[cell wall synthesis|cell wall metabolism]] | ||
Revision as of 08:30, 6 August 2015
Welcome to SubtiWiki! - Bacillus subtilis annotation the "wiki" way!
Contact: General Microbiology, University of Göttingen, send mail
Upcoming events:
- The 8th International Conference on Gram-positive Microorganisms (18th International Conference on Bacilli) in Montecatini Terme, organized by Marta Perego will take place from June 21 to 25. Conference website
- The 7th European Spores Conference, organized by Simon Cutting and Imrich Barak, will take place from April 18 to 20, 2016, at Royal Holloway, University of London. Conference website
- Past conferences
New: Subtiwiki is now on Facebook - please give it a +1!
Now online: A new description of SubtiWiki and its acompanying modules in the 2014 Database issue of Nucleic Acids Research
Raphael H Michna, Fabian M Commichau, Dominik Tödter, Christopher P Zschiedrich, Jörg Stülke
SubtiWiki-a database for the model organism Bacillus subtilis that links pathway, interaction and expression information.
Nucleic Acids Res: 2014, 42(Database issue);D692-8
[PubMed:24178028]
[WorldCat.org]
[DOI]
(I p)
Paper of the month: July 2015
- The precise functions of serine protein kinases in B. subtilis have largely remained enigmatic until very recently. Now, two studies from the lab of Jonathan Dworkin describe functions and molecular targets for two of these kinases, PrkC and YabT. Pereira et al. have identified the universally conserved elongation factor Tu as a target for the protein kinase YabT. In srarving cells, YabT phosphorylates EF-Tu at a conserved threonine residue. Phosphorylation impairs the essential GTPase activity of EF-Tu, thereby preventing its release from the ribosome. As a consequence, phosphorylated EF-Tu has a dominant-negative effect in translation elongation, resulting in the overall inhibition of protein synthesis. Importantly, this mechanism allows a quick and robust regulation of one of the most abundant cellular proteins. Libby et al. have uncovered that phosphorylation by PrkC stimulates the activity of the essential two-component transcription factor WalR. This mechanism links the presence of muropeptides that trigger PrkC activity to the expression of the genes of the WalR regulon that are involved in cell wall metabolism.
- Relevant SubtiWiki pages: Jonathan Dworkin, protein kinases, YabT, EF-Tu, PrkC, WalR, cell wall metabolism
Elizabeth A Libby, Lindsie A Goss, Jonathan Dworkin
The Eukaryotic-Like Ser/Thr Kinase PrkC Regulates the Essential WalRK Two-Component System in Bacillus subtilis.
PLoS Genet: 2015, 11(6);e1005275
[PubMed:26102633]
[WorldCat.org]
[DOI]
(I e)
Sandro F F Pereira, Ruben L Gonzalez, Jonathan Dworkin
Protein synthesis during cellular quiescence is inhibited by phosphorylation of a translational elongation factor.
Proc Natl Acad Sci U S A: 2015, 112(25);E3274-81
[PubMed:26056311]
[WorldCat.org]
[DOI]
(I p)
New procedure for account creation:
- Due to massive spam attacks, we had to change our policy for the creation of accounts. If you want to create an account, just send me a mail. We will create the account for you as quickly as possible, then you can change your password. This does not affect existing accounts, which remain active.
- Please remember that all members of the Bacillus community are invited to create accounts and to contribute to SubtiWiki!
News in SubtiWiki:
- August 2014: The first mobile application for SubtiWiki is now available for users of Android phones: Go for SubtiWiki in Google Play! IPhone users, please be patient! You will be served next! Click here to install!
- April 2013: SubtiWiki uses a new, faster Mediawiki platform! The times for page access are significantly reduced. Enjoy!
- March 2013: updated Excel files that map all genes to categories and regulons as well as the general updated identity mapping of all genes were uploaded.
- October 2012: the essential genes have been categorized
- September 2012: 300 mutant strains available at the BGSC were added to the corresponding gene pages
- August 2012: SubtiExpress, the new compagnon of SubtiWiki devoted to gene expression is online! Try it out!
- April 2012: Links for expression data under 104 different conditions (based on Nicolas et al., 2012) have been added to the expression section of the individual gene pages
- April 2011: SubtInteract, a presentation of protein-protein interactions in B. subtilis, is online!
- December 2010: SubtiCellPublisher allows the conversion of CellDesigner diagrams to navigatable presentations in the style of SubtiPathways
| Genes (examples) | Additional pages |
| spo0A | SubtiPathways |
| glnA | SubtInteract |
| rny | SubtiExpress |
| psdA | Regulons |
| pckA | methods |
| dnaA | metabolism |
| rnpA | categories |
| sigB | genome-wide analyses |
| ptkA | list of plasmids |
| mreC | labs working on Bacillus |
| ccpA | the people behind SubtiWiki |
| sr1 | template |
Publications describing SubtiWiki and SubtiPathways:
