Difference between revisions of "Papers of the month"

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(2011)
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  <big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J''  </big>
 
  <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>'''RNA processing in ''Bacillus subtilis'': identification of targets of the essential RNase Y.''' </big>
  <big>Mol Microbiol. 2011 Aug 4. doi: 10.1111/j.1365-2958.2011.07777.x. [Epub ahead of print] </big>
+
  <big>Mol Microbiol. 2011 81(6): 1459-73. </big>
 
  [http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947]
 
  [http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947]
 
<pubmed>21803996 21843271 </pubmed>
 
<pubmed>21803996 21843271 </pubmed>

Revision as of 09:03, 3 October 2011

2011

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

Patrice Bruscella, Karen Shahbabian, Soumaya Laalami, Harald Putzer
RNase Y is responsible for uncoupling the expression of translation factor IF3 from that of the ribosomal proteins L35 and L20 in Bacillus subtilis.
Mol Microbiol: 2011, 81(6);1526-41
[PubMed:21843271] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Joseph Newman, Fabian M Rothe, Alexandra S Solovyova, Cecilia Rodrigues, Christina Herzberg, Fabian M Commichau, Richard J Lewis, Jörg Stülke
RNase Y in Bacillus subtilis: a Natively disordered protein that is the functional equivalent of RNase E from Escherichia coli.
J Bacteriol: 2011, 193(19);5431-41
[PubMed:21803996] [WorldCat.org] [DOI] (I p)


Bui Khanh Chi, Katrin Gronau, Ulrike Mäder, Bernd Hessling, Dörte Becher, Haike Antelmann
S-bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics.
Mol Cell Proteomics: 2011, 10(11);M111.009506
[PubMed:21749987] [WorldCat.org] [DOI] (I p)


  • 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

Zachary D Miles, Reid M McCarty, Gabriella Molnar, Vahe Bandarian
Discovery of epoxyqueuosine (oQ) reductase reveals parallels between halorespiration and tRNA modification.
Proc Natl Acad Sci U S A: 2011, 108(18);7368-72
[PubMed:21502530] [WorldCat.org] [DOI] (I p)