Difference between revisions of "MreB"

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(Reviews)
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* '''Description:''' cell-shape determining protein, forms filaments <br/><br/>
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* '''Description:''' [[cell shape]]-determining protein, forms filaments, the polymers control/restrict the mobility of the cell wall elongation enzyme complex <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Essential''' || yes [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || yes [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Product''' || cell-shape determining protein
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|style="background:#ABCDEF;" align="center"| '''Product''' || [[cell shape]]-determining protein
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Function''' || cell-shape determination  
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|style="background:#ABCDEF;" align="center"|'''Function''' || [[cell shape]] determination  
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 35 kDa, 4.901   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 35 kDa, 4.901   
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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
 
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* essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed], the mutation can be suppressed by inactivation of ''[[ponA]]'', ''[[ptsI]]'', ''[[ccpA]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/19192185 PubMed], by overexpression of [[YvcK]] {{PubMed|21320184}}, or by addition of 5 mM magnesium to the growth medium [http://www.ncbi.nlm.nih.gov/pubmed/15752190 PubMed]
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* the mutation can be suppressed by inactivation of ''[[ponA]]'', ''[[ptsI]]'', ''[[ccpA]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/19192185 PubMed], by overexpression of [[YvcK]] {{PubMed|21320184}}, or by addition of 5 mM magnesium to the growth medium [http://www.ncbi.nlm.nih.gov/pubmed/15752190 PubMed]
  
 
=== Database entries ===
 
=== Database entries ===
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=== Additional information===
 
=== Additional information===
 
 
  
  
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
* '''Interactions:''' [[MreB]]-[[TufA]] {{PubMed|20133608}}, [[MreB]]-[[Mbl]], [[MreB]]-[[MreBH]] [http://www.ncbi.nlm.nih.gov/sites/entrez/17064365 PubMed]
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* '''[[SubtInteract|Interactions]]:'''
 +
** part of the [[cell wall biosynthetic complex]] {{PubMed|21636744,21636745}}
 +
** [[MreB]]-[[TufA]] {{PubMed|20133608}}
 +
** [[MreB]]-[[Mbl]] {{PubMed|21636744}}
 +
** [[MreB]]-[[MreBH]] {{PubMed|21636744,17064365}}
  
 
* '''Localization:'''  
 
* '''Localization:'''  
** forms helical structures close to the inner surface of the cytoplasmic membrane [http://www.ncbi.nlm.nih.gov/sites/entrez/16950129 PubMed]
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** during logarithmic growth, [[MreB]] forms discrete patches thst move processively along peripheral tracks perpendicular to the cell axis {{PubMed|21636744}}
** formation of helical clusters depends on the proton motive force {{PubMed|20566861}}  
+
** forms transverse bands as cells enter the stationary phase {{PubMed|21636744}}
 +
** close to the inner surface of the cytoplasmic membrane [http://www.ncbi.nlm.nih.gov/sites/entrez/16950129 PubMed]
 +
** reports on helical structures formed by MreB {{PubMed|16950129,20566861}} seem to be misinterpretation of data {{PubMed|21636744}}
  
 
=== Database entries ===
 
=== Database entries ===

Revision as of 05:19, 11 July 2011

  • Description: cell shape-determining protein, forms filaments, the polymers control/restrict the mobility of the cell wall elongation enzyme complex

Gene name mreB
Synonyms divIVB
Essential yes PubMed
Product cell shape-determining protein
Function cell shape determination
MW, pI 35 kDa, 4.901
Gene length, protein length 1011 bp, 337 aa
Immediate neighbours mreC, radC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
MreB context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

cell shape, cell envelope stress proteins (controlled by SigM, W, X, Y), essential genes, membrane proteins

This gene is a member of the following regulons

SigM regulon

The gene

Basic information

  • Locus tag: BSU28030

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • forms straight filaments in a heterologous system PubMed
    • polymerizes in the presence of millimolar divalent cations, binds and hydrolyzes GTP and ATP PubMed
  • Protein family: ftsA/mreB family (according to Swiss-Prot)

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:
    • during logarithmic growth, MreB forms discrete patches thst move processively along peripheral tracks perpendicular to the cell axis PubMed
    • forms transverse bands as cells enter the stationary phase PubMed
    • close to the inner surface of the cytoplasmic membrane PubMed
    • reports on helical structures formed by MreB PubMed seem to be misinterpretation of data PubMed

Database entries

  • Structure: 1JCE (from Thermotoga maritima) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:

Labs working on this gene/protein

Jeff Errington, Newcastle University, UK homepage

Peter Graumann, Freiburg University, Germany homepage

Your additional remarks

References

Reviews

Additional reviews: PubMed

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

Peter L Graumann
Cytoskeletal elements in bacteria.
Annu Rev Microbiol: 2007, 61;589-618
[PubMed:17506674] [WorldCat.org] [DOI] (P p)

Rut Carballido-López
The bacterial actin-like cytoskeleton.
Microbiol Mol Biol Rev: 2006, 70(4);888-909
[PubMed:17158703] [WorldCat.org] [DOI] (P p)

Linda A Amos, Fusinita van den Ent, Jan Löwe
Structural/functional homology between the bacterial and eukaryotic cytoskeletons.
Curr Opin Cell Biol: 2004, 16(1);24-31
[PubMed:15037301] [WorldCat.org] [DOI] (P p)


Localization

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)

Henrik Strahl, Leendert W Hamoen
Membrane potential is important for bacterial cell division.
Proc Natl Acad Sci U S A: 2010, 107(27);12281-6
[PubMed:20566861] [WorldCat.org] [DOI] (I p)

Hervé Joël Defeu Soufo, Peter L Graumann
Dynamic localization and interaction with other Bacillus subtilis actin-like proteins are important for the function of MreB.
Mol Microbiol: 2006, 62(5);1340-56
[PubMed:17064365] [WorldCat.org] [DOI] (P p)


Other original publications