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>  
  
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==Complex members==
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* cell wall biosynthetic enzymes at the outer side of the membrane: [[penicillin-binding proteins]] ([[PbpA]], [[PbpH]], perhaps also [[PbpC]], [[DacC]], [[PbpI]])
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* transmembrane proteins: [[MreC]], [[MreD]], [[RodA]], [[RodZ]], they couple the cytosolic actin-like proteins to the extracellular peptidoglycan-synthesizing machinery
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* 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==
 
==Related pages==
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* [[cell wall synthesis]]
 
* [[cell wall synthesis]]
 
* [http://subtiwiki.uni-goettingen.de/pathways/cellwall.html Cell wall synthesis in SubtiPathways]
 
* [http://subtiwiki.uni-goettingen.de/pathways/cellwall.html Cell wall synthesis in SubtiPathways]
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==Labs working on the complex==
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* [[Rut Carballido-Lopez]], Jouy-en-Josas
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* [[Jeff Errington]], Newcastle upon Tyne
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* [[David Rudner]], New York
  
 
==Important publications==
 
==Important publications==
* [http://www.ncbi.nlm.nih.gov/pubmed/21636744 Domínguez-Escobar ''et al''.] from [[Rut Carballido-Lopez]]' lab and [http://www.ncbi.nlm.nih.gov/pubmed/21636745 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<br/>
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<pubmed>21636744 21636745 23848140 21725336 24094808 26029191</pubmed>
* '''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]]
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<pubmed>21636744 21636745</pubmed>
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==Back to [[SubtInteract]]==
* A comment on these papers:
 
<pubmed> 21725336 </pubmed>
 

Latest revision as of 15:33, 7 July 2015

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 (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

Important publications

Alexander J F Egan, Waldemar Vollmer
The stoichiometric divisome: a hypothesis.
Front Microbiol: 2015, 6;455
[PubMed:26029191] [WorldCat.org] [DOI] (P e)

Piotr Szwedziak, Jan Löwe
Do the divisome and elongasome share a common evolutionary past?
Curr Opin Microbiol: 2013, 16(6);745-51
[PubMed:24094808] [WorldCat.org] [DOI] (I p)

Orietta Massidda, Linda Nováková, Waldemar Vollmer
From models to pathogens: how much have we learned about Streptococcus pneumoniae cell division?
Environ Microbiol: 2013, 15(12);3133-57
[PubMed:23848140] [WorldCat.org] [DOI] (I p)

Andrew Jermy
Bacterial physiology: MreB takes a back seat.
Nat Rev Microbiol: 2011, 9(8);560-1
[PubMed:21725336] [WorldCat.org] [DOI] (I e)

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)


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