Difference between revisions of "Elongasome"
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==Complex members== | ==Complex members== | ||
* cell wall biosynthetic enzymes at the outer side of the membrane: [[penicillin-binding proteins]] | * cell wall biosynthetic enzymes at the outer side of the membrane: [[penicillin-binding proteins]] | ||
| − | * transmembrane proteins: [[MreC]], [[MreD]] | + | * transmembrane proteins: [[MreC]], [[MreD]], [[RodA]], [[RodZ]] |
* actin-like proteins at the inner surface of the membrane: [[MreB]], [[MreBH]], [[Mbl]] | * actin-like proteins at the inner surface of the membrane: [[MreB]], [[MreBH]], [[Mbl]] | ||
| − | |||
==Related pages== | ==Related pages== | ||
Revision as of 04:52, 11 July 2011
A protein complex that catalyzes peptidoglycan biosynthesis and is thereby involved in maintaining cell shape
Contents
Complex members
- cell wall biosynthetic enzymes at the outer side of the membrane: penicillin-binding proteins
- transmembrane proteins: MreC, MreD, RodA, RodZ
- actin-like proteins at the inner surface of the membrane: MreB, MreBH, Mbl
Related pages
Labs working on the complex
- Rut Carballido-Lopez, Jouy-en-Josas
- Jeff Errington, Newcastle upon Tyne
- David Rudner, New York
Important publications
- 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:
