Difference between revisions of "Papers of the month"
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+ | * '''October 2011''' | ||
+ | ** [http://www.ncbi.nlm.nih.gov/pubmed/21925382 Richards ''et al''.] identify the [[nudix hydrolase]] [[RppH]] as the pyrophosphohydrolase that triggers 5'-exonucleolytic degradation of mRNA by [[rnjA|RNase J1]] in ''B. subtilis''. | ||
+ | ** '''Relevant ''Subti''Wiki pages:''' [[David Bechhofer]], [[Ciaran Condon]], [[RNases|RNA processing and degradation]], [[nudix hydrolase]], [[RppH]], [[rnjA|RNase J1]] | ||
+ | <pubmed>21925382</pubmed> | ||
+ | |||
* '''September 2011''' | * '''September 2011''' | ||
** 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. |
Revision as of 09:09, 3 October 2011
2011
- October 2011
- Richards et al. identify the nudix hydrolase RppH as the pyrophosphohydrolase that triggers 5'-exonucleolytic degradation of mRNA by RNase J1 in B. subtilis.
- Relevant SubtiWiki pages: David Bechhofer, Ciaran Condon, RNA processing and degradation, nudix hydrolase, RppH, RNase J1
- September 2011
- A series of papers deals with RNA processing and degradation in B. subtilis. Three papers establish that RNase Y is the functional equivalent of RNase E from E. coli. Moreover, the role of RNase J1 in endonucleolytic cleavage of the trp leader mRNA is demonstrated.
- Relevant SubtiWiki pages: David Bechhofer, Rick Lewis, Ulrike Mäder, Harald Putzer, Jörg Stülke, RNases, RNA degradosome, RNase Y, RNase Y targets, RNase J1
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
- August 2011
- Chi et al. demonstrate that S-bacillithiolation of the repressor OhrR and of four enzymes of the methionine biosynthesis pathway protects the B. subtilis cell against hypochlorite stress.
- Relevant SubtiWiki pages: Haike Antelmann, Dörte Becher, Ulrike Mäder, resistance against oxidative and electrophile stress, Spx regulon, CtsR regulon, PerR regulon, OhrR, MetE, YxjG, PpaC, SerA, YphP
- July 2011
- Domínguez-Escobar et al. from Rut Carballido-Lopez' lab and Garner et al. report that movement of actin-like filaments is driven by the peptidoglycan elongation machinery. Both papers suggest that the MreB-like filaments serve to restrict the mobility of the peptidoglycan synthesizing machinery
- Relevant SubtiWiki pages: Rut Carballido-Lopez, David Rudner, MreB, MreBH, Mbl, MreC, MreD, PbpA, RodA, RodZ, penicillin-binding proteins, cell shape, cell wall synthesis, cell wall biosynthetic complex
- Domínguez-Escobar et al. from Rut Carballido-Lopez' lab and Garner et al. report that movement of actin-like filaments is driven by the peptidoglycan elongation machinery. Both papers suggest that the MreB-like filaments serve to restrict the mobility of the peptidoglycan synthesizing machinery
- A comment on these papers:
Andrew Jermy
Bacterial physiology: MreB takes a back seat.
Nat Rev Microbiol: 2011, 9(8);560-1
[PubMed:21725336]
[WorldCat.org]
[DOI]
(I e)
- June 2011
- Oppenheimer-Shaanan et al. from Sigal Ben-Yehuda's lab report that cyclic di-AMP acts as a secondary messenger that couples DNA integrity with progression of sporulation
- Relevant SubtiWiki pages: Sigal Ben-Yehuda, DisA, YybT, metabolism of signalling nucleotides, cell division
- Oppenheimer-Shaanan et al. from Sigal Ben-Yehuda's lab report that cyclic di-AMP acts as a secondary messenger that couples DNA integrity with progression of sporulation
- 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
- 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