Difference between revisions of "Papers of the month"

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(2013)
(2013)
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** '''Relevant ''Subti''Wiki pages:'''  [[David Rudner]], [[FisB]], [[sporulation]]
 
** '''Relevant ''Subti''Wiki pages:'''  [[David Rudner]], [[FisB]], [[sporulation]]
 
<pubmed> 23388828 </pubmed>
 
<pubmed> 23388828 </pubmed>
** See also:
+
* See also:
 
<pubmed> 23518060 </pubmed>
 
<pubmed> 23518060 </pubmed>
  
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** For many [[essential genes]] of ''B. subtilis'', it is not clear why they are essential in ''B. subtilis'' but not in closely related species. Strikingly, this is the case for [[RNases]] such as RNases [[rnc|III]] and [[rny|Y]]. Now, [http://www.ncbi.nlm.nih.gov/pubmed/23300471 Durand et al..] from the lab of [[Ciaran Condon]] have identified the reason for the essentiality of [[rnc|RNase III]]: This enzyme is required to degrade phage encoded toxin mRNA molecules thus protecting the cell from lysis caused by the encoded toxins. Indeed, [[rnc|RNase III]] is dispensable in a strain lacking the [[Skin element]] and the [[SPß prophage]] that harbor the corresponding toxin genes.
 
** For many [[essential genes]] of ''B. subtilis'', it is not clear why they are essential in ''B. subtilis'' but not in closely related species. Strikingly, this is the case for [[RNases]] such as RNases [[rnc|III]] and [[rny|Y]]. Now, [http://www.ncbi.nlm.nih.gov/pubmed/23300471 Durand et al..] from the lab of [[Ciaran Condon]] have identified the reason for the essentiality of [[rnc|RNase III]]: This enzyme is required to degrade phage encoded toxin mRNA molecules thus protecting the cell from lysis caused by the encoded toxins. Indeed, [[rnc|RNase III]] is dispensable in a strain lacking the [[Skin element]] and the [[SPß prophage]] that harbor the corresponding toxin genes.
 
** '''Relevant ''Subti''Wiki pages:'''  [[Ciaran Condon]], [[rnc|RNase III]], [[essential genes]], ''[[yonT]]'', ''[[txpA]]'', [[toxins, antitoxins and immunity against toxins]]
 
** '''Relevant ''Subti''Wiki pages:'''  [[Ciaran Condon]], [[rnc|RNase III]], [[essential genes]], ''[[yonT]]'', ''[[txpA]]'', [[toxins, antitoxins and immunity against toxins]]
<big>''Durand S, Gilet L, Condon C''  </big>
+
<pubmed> 23300471 </pubmed>
<big>'''The essential function of ''B. subtilis'' RNase III is to silence foreign toxin genes.''' </big>
+
* '''A comment on this paper:'''
<big>PLoS Genet. 2012 8(12): e1003181.</big>
 
[http://www.ncbi.nlm.nih.gov/pubmed/23300471 PubMed:23300471]
 
** '''A comment on this paper:'''
 
 
<pubmed> 23300472 </pubmed>
 
<pubmed> 23300472 </pubmed>
** '''See also:'''
+
* '''See also:'''
 
<pubmed> 23059907 </pubmed>
 
<pubmed> 23059907 </pubmed>
  

Revision as of 15:07, 27 March 2013

2013

  • March 2013
    • The mechanism of membrane fission in bacteria has been a long-standing enigma. Now, Doan et al.. from the lab of David Rudner demonstrate how the FisB protein (previously YunB) mediates membrane fission during sporulation This activity of FisB is based on its ability to bind to lipids, specifically to cardiolipin..
    • Relevant SubtiWiki pages: David Rudner, FisB, sporulation

  • See also:


  • A comment on this paper:

  • See also:



2012

  • December 2012
    • Kim et al.. show how the ATP hydrolysis controls the global conformation of the SecA translocase and drives protein secretion. The intricate network of structural interactions, which couple local electrostatic changes during ATP hydrolysis to global conformational and dynamic changes in SecA, form the foundation of the allosteric mechanochemistry that efficiently harnesses the chemical energy stored in ATP to drive complex mechanical processes.
    • Relevant SubtiWiki pages: SecA, protein secretion









Levdikov VM, Blagova EV, McFeat A, Fogg MJ, Wilson KS, Wilkinson AJ  
Structure of components of an intercellular channel complex in sporulating Bacillus subtilis. 
Proc Natl Acad Sci U S A. 2012, 109(14):5441-5. 
PubMed:22431604


  • A comment on these papers:


  • A comment on this paper:



2011


Locke JC, Young JW, Fontes M, Hernández Jiménez MJ, Elowitz MB  
Stochastic pulse regulation in bacterial stress response. 
Science. 2011 334:366-369. 
PubMed:21979936



Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-73. 
PubMed:21815947



  • A comment on these papers:



  • May 2011
    • Miles et al. identified the enzyme for the key final step in the biosynthesis of queuosine, a hypermodified base found in the wobble positions of tRNA Asp, Asn, His, and Tyr from bacteria to man
    • Relevant SubtiWiki pages: QueG, translation