Difference between revisions of "Elongasome"
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<big>'''A protein complex that catalyzes peptidoglycan biosynthesis and is thereby involved in maintaining [[cell shape]]'''</big> | <big>'''A protein complex that catalyzes peptidoglycan biosynthesis and is thereby involved in maintaining [[cell shape]]'''</big> | ||
+ | ==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== | ==Related pages== |
Revision as of 19:02, 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)