Difference between revisions of "Papers of the month"
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| + | * '''August 2011''' | ||
| + | ** [http://www.ncbi.nlm.nih.gov/pubmed/21749987 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. | ||
| + | <pubmed>21749987</pubmed> | ||
| + | ** '''Relevant ''Subti''Wiki 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]] | ||
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* '''July 2011''' | * '''July 2011''' | ||
** [http://www.ncbi.nlm.nih.gov/pubmed/21636744 Domínguez-Escobar ''et al''.] from [[Rut Carballido-Lopez]]' lab and [http://www.ncbi.nlm.nih.gov/pubmed/21636745 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<br/> | ** [http://www.ncbi.nlm.nih.gov/pubmed/21636744 Domínguez-Escobar ''et al''.] from [[Rut Carballido-Lopez]]' lab and [http://www.ncbi.nlm.nih.gov/pubmed/21636745 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<br/> | ||
Revision as of 18:21, 30 July 2011
2011
- 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
Ethan C Garner, Remi Bernard, Wenqin Wang, Xiaowei Zhuang, David Z Rudner, Tim Mitchison
Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis.
Science: 2011, 333(6039);222-5
[PubMed:21636745]
[WorldCat.org]
[DOI]
(I p)
Julia Domínguez-Escobar, Arnaud Chastanet, Alvaro H Crevenna, Vincent Fromion, Roland Wedlich-Söldner, Rut Carballido-López
Processive movement of MreB-associated cell wall biosynthetic complexes in bacteria.
Science: 2011, 333(6039);225-8
[PubMed:21636744]
[WorldCat.org]
[DOI]
(I p)
- A comment on these papers:
- 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
