Difference between revisions of "Papers of the month"

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(2013)
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** [http://www.ncbi.nlm.nih.gov/pubmed/22431613 Meisner ''et al''.] and [http://www.ncbi.nlm.nih.gov/pubmed/22431604 Levdikov ''et al''.] from the labs of [[Charles Moran]] and [[Tony Wilkinson]], respectively, have reported the structure of the complex between [[SpoIIQ]] and [[SpoIIIAH]]. These two proteins interact through two membranes to connect the forespore and the mother cell during [[sporulation proteins|sporulation]]. The structure of the complex suggests that it is the extracellular component of a gap junction-like intercellular channel for the traffic of proteins between the two compartments.
 
** [http://www.ncbi.nlm.nih.gov/pubmed/22431613 Meisner ''et al''.] and [http://www.ncbi.nlm.nih.gov/pubmed/22431604 Levdikov ''et al''.] from the labs of [[Charles Moran]] and [[Tony Wilkinson]], respectively, have reported the structure of the complex between [[SpoIIQ]] and [[SpoIIIAH]]. These two proteins interact through two membranes to connect the forespore and the mother cell during [[sporulation proteins|sporulation]]. The structure of the complex suggests that it is the extracellular component of a gap junction-like intercellular channel for the traffic of proteins between the two compartments.
 
** '''Relevant ''Subti''Wiki pages:'''  [[Charles Moran]], [[Tony Wilkinson]], [[sporulation proteins|sporulation]], [[SpoIIQ]], [[SpoIIIAH]]
 
** '''Relevant ''Subti''Wiki pages:'''  [[Charles Moran]], [[Tony Wilkinson]], [[sporulation proteins|sporulation]], [[SpoIIQ]], [[SpoIIIAH]]
<big>''Levdikov VM, Blagova EV, McFeat A, Fogg MJ, Wilson KS, Wilkinson AJ''  </big>
+
<pubmed> 22431613 22431604 </pubmed>
<big>'''Structure of components of an intercellular channel complex in sporulating ''Bacillus subtilis''.''' </big>
 
<big>Proc Natl Acad Sci U S A. 2012, 109(14):5441-5. </big>
 
[http://www.ncbi.nlm.nih.gov/pubmed/22431604 PubMed:22431604]
 
<pubmed> 22431613</pubmed>
 
  
 
* '''March 2012'''
 
* '''March 2012'''
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** [http://www.ncbi.nlm.nih.gov/pubmed/21979936 Locke ''et al''.] show how the [[SigB]]-dependent general stress response is controlled by signals using stochastic pulse frequency modulation through a compact regulatory architecture.
 
** [http://www.ncbi.nlm.nih.gov/pubmed/21979936 Locke ''et al''.] show how the [[SigB]]-dependent general stress response is controlled by signals using stochastic pulse frequency modulation through a compact regulatory architecture.
 
** '''Relevant ''Subti''Wiki pages:'''  [[Michael Elowitz]], [[SigB]], [[General stress proteins (controlled by SigB)|General stress response]]  
 
** '''Relevant ''Subti''Wiki pages:'''  [[Michael Elowitz]], [[SigB]], [[General stress proteins (controlled by SigB)|General stress response]]  
<big>''Locke JC, Young JW, Fontes M, Hernández Jiménez MJ, Elowitz MB''  </big>
+
<pubmed> 21979936 </pubmed>
<big>'''Stochastic pulse regulation in bacterial stress response.''' </big>
 
<big>Science. 2011 334:366-369. </big>
 
[http://www.ncbi.nlm.nih.gov/pubmed/21979936 PubMed:21979936]
 
  
  
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** A series of papers deals with [[RNases|RNA processing and degradation]] in ''B. subtilis''. Three papers establish that [[rny|RNase Y]] is the functional equivalent of RNase E from ''E. coli''. Moreover, the role of [[rnjA|RNase J1]] in endonucleolytic cleavage of the trp leader mRNA is demonstrated.
 
** A series of papers deals with [[RNases|RNA processing and degradation]] in ''B. subtilis''. Three papers establish that [[rny|RNase Y]] is the functional equivalent of RNase E from ''E. coli''. Moreover, the role of [[rnjA|RNase J1]] in endonucleolytic cleavage of the trp leader mRNA is demonstrated.
 
** '''Relevant ''Subti''Wiki pages:'''  [[David Bechhofer]], [[Rick Lewis]], [[Ulrike Mäder]], [[Harald Putzer]], [[Jörg Stülke]], [[RNases]], [[RNA degradosome]], [[rny|RNase Y]],  [[RNase Y targets]], [[rnjA|RNase J1]]
 
** '''Relevant ''Subti''Wiki pages:'''  [[David Bechhofer]], [[Rick Lewis]], [[Ulrike Mäder]], [[Harald Putzer]], [[Jörg Stülke]], [[RNases]], [[RNA degradosome]], [[rny|RNase Y]],  [[RNase Y targets]], [[rnjA|RNase J1]]
<pubmed>21862575 </pubmed>
+
<pubmed>21862575 21815947 21803996 21843271 </pubmed>
<big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J''  </big>
 
<big>'''RNA processing in ''Bacillus subtilis'': identification of targets of the essential RNase Y.''' </big>
 
<big>Mol Microbiol. 2011 81(6): 1459-73. </big>
 
[http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947]
 
<pubmed>21803996 21843271 </pubmed>
 
 
 
  
 
* '''August 2011'''
 
* '''August 2011'''

Revision as of 17:30, 13 July 2013

2013

  • July 2013
    • Ca(2+) efflux by Ca(2+) cation antiporter (CaCA) proteins is important for maintenance of Ca(2+) homeostasis across the cell membrane. Now, Wu et al. determined the structure of the B. subtilis Ca(2+)/H(+) antiporter protein ChaA. By structural and mutational analyses, they establish structural bases for mechanisms of Ca(2+)/H(+) exchange and its pH regulation. Moreover, this work also sheds light on the evolutionary adaptation to different energy modes in the CaCA protein family.
    • Relevant SubtiWiki pages: ChaA, membrane proteins, metal ion homeostasis (K, Na, Ca, Mg)


  • June 2013
    • DNA transfer across membranes is important in many fundamental processes. However, the molecular mechanisms behind this transport are only poorly understood. Now, Fiche et al. analysed the assembly and molecular architecture of the SpoIIIE DNA translocation complex. This study reveals that in contrast to previous model, DNA transfer occurs through an aqueous DNA-conducting pore that could be structurally maintained by the divisional machinery, with SpoIIIE acting as a checkpoint preventing membrane fusion until completion of chromosome segregation.
    • Relevant SubtiWiki pages: sporulation, SpoIIIE, DNA condensation/ segregation


  • May 2013
    • Paul et al. demonstrate that the orientation of the genes on the chromosome has a significant impact on their evolution: Gene encoded on the lagging strand evolve faster than those on the leading strand. This faster evolution is caused by collisions between the DNA replication and transcription machineries that result in DNA damage and subsequent fixation of errors as mutations. Importantly, essential genes are strongly underrepresented on the lagging strand thus providing a "built-in" protection of the encoded important proteins against possible deleterious mutations.
    • Relevant SubtiWiki pages: transcription, DNA replication, essential genes



  • 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

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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










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2011






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  • 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