Difference between revisions of "Papers of the month"

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=2012=
 
=2012=
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* '''May 2012'''
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** [http://www.ncbi.nlm.nih.gov/pubmed/22517742 Elsholz''et al''.] from the lab of [[Ulf Gerth]] demonstrate that protein phosphorylation on arginine residues is of great importance for B. subtilis. In addition to the previously identified target [[CtsR]], 86 proteins are shown to be  phosphorylated on arginine. The protein arginine kinase and phosphatase, McsB and YwlE, respectively, may thus have an important regulatory role in ''B. subtilis''.
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** '''Relevant ''Subti''Wiki pages:'''  [[Ulf Gerth]], [[Kürsad Turgay]], [[Ulrike Mäder]], [[Dörte Becher]], [[Michael Hecker]], [[phosphoproteins]], [[protein kinases and phosphatases]], [[McsB]], [[YwlE]]
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<pubmed>22517742</pubmed>
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* '''April 2012'''
 
* '''April 2012'''
 
** [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.

Revision as of 15:28, 29 April 2012

2012

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)


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 Mar 19. [Epub ahead of print] 
PubMed:22431604


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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


Jamie Richards, Quansheng Liu, Olivier Pellegrini, Helena Celesnik, Shiyi Yao, David H Bechhofer, Ciarán Condon, Joel G Belasco
An RNA pyrophosphohydrolase triggers 5'-exonucleolytic degradation of mRNA in Bacillus subtilis.
Mol Cell: 2011, 43(6);940-9
[PubMed:21925382] [WorldCat.org] [DOI] (I p)


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



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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