Difference between revisions of "Papers of the month"
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** '''Relevant ''Subti''Wiki pages:''' [[Rut Carballido-Lopez]], [[David Rudner]], [[MreB]], [[MreBH]], [[Mbl]], [[MreC]], [[MreD]], [[PbpA]], [[RodA]], [[RodZ]], [[penicillin-binding proteins]], [[cell shape]], [[cell wall synthesis]] | ** '''Relevant ''Subti''Wiki pages:''' [[Rut Carballido-Lopez]], [[David Rudner]], [[MreB]], [[MreBH]], [[Mbl]], [[MreC]], [[MreD]], [[PbpA]], [[RodA]], [[RodZ]], [[penicillin-binding proteins]], [[cell shape]], [[cell wall synthesis]] | ||
<pubmed>21636744 21636745</pubmed> | <pubmed>21636744 21636745</pubmed> | ||
+ | * A comment on these papers: | ||
+ | <pubmed> 21725336 </pubmed> | ||
* '''June 2011''' | * '''June 2011''' |
Revision as of 16:46, 7 July 2011
2011
- 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
- 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:
- 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