Difference between revisions of "Elongasome"
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* A comment on these papers: | * A comment on these papers: | ||
<pubmed> 21725336 </pubmed> | <pubmed> 21725336 </pubmed> | ||
| + | |||
| + | ==Labs working on the complex== | ||
| + | * [[Rut Carballido-Lopez]], Jouy-en-Josas | ||
| + | * [[Jeff Errington]], Newcastle upon Tyne | ||
| + | * [[David Rudner]], New York | ||
Revision as of 19:04, 10 July 2011
A protein complex that catalyzes peptidoglycan biosynthesis and is thereby involved in maintaining cell shape
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
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
- Relevant SubtiWiki pages: Rut Carballido-Lopez, David Rudner, MreB, MreBH, Mbl, MreC, MreD, PbpA, RodA, RodZ, penicillin-binding proteins, cell shape, cell wall synthesis
- 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)
Labs working on the complex
- Rut Carballido-Lopez, Jouy-en-Josas
- Jeff Errington, Newcastle upon Tyne
- David Rudner, New York
