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]] ([[PbpA]], [[PbpH]]) | + | * cell wall biosynthetic enzymes at the outer side of the membrane: [[penicillin-binding proteins]] ([[PbpA]], [[PbpH]], perhaps also [[PbpC]], [[DacC]], [[PbpI]]) |
* transmembrane proteins: [[MreC]], [[MreD]], [[RodA]], [[RodZ]], they couple the cytosolic actin-like proteins to the extracellular peptidoglycan-synthesizing machinery | * transmembrane proteins: [[MreC]], [[MreD]], [[RodA]], [[RodZ]], they couple the cytosolic actin-like proteins to the extracellular peptidoglycan-synthesizing machinery | ||
* actin-like proteins at the inner surface of the membrane: [[MreB]], [[MreBH]], [[Mbl]], the polymers control/restrict the mobility of the cell wall elongation enzyme complex | * actin-like proteins at the inner surface of the membrane: [[MreB]], [[MreBH]], [[Mbl]], the polymers control/restrict the mobility of the cell wall elongation enzyme complex | ||
Revision as of 18:32, 13 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 (PbpA, PbpH, perhaps also PbpC, DacC, PbpI)
- transmembrane proteins: MreC, MreD, RodA, RodZ, they couple the cytosolic actin-like proteins to the extracellular peptidoglycan-synthesizing machinery
- actin-like proteins at the inner surface of the membrane: MreB, MreBH, Mbl, the polymers control/restrict the mobility of the cell wall elongation enzyme complex
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
- A comment on these papers:
