Difference between revisions of "Mbl"

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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''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Product''' || MreB-like protein
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|style="background:#ABCDEF;" align="center"| '''Product''' || [[MreB]]-like 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, 5.669   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 35 kDa, 5.669   
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
* '''Interactions:''' [[MreB]]-[[Mbl]], [[Mbl]]-[[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]]-[[Mbl]] {{PubMed|21636744}}
 +
** [[Mbl]]-[[MreBH]] [http://www.ncbi.nlm.nih.gov/sites/entrez/17064365 PubMed]
  
 
* '''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, [[Mbl]] 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}}  
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** 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 Mbl {{PubMed|16950129,20566861}} seem to be misinterpretation of data {{PubMed|21636744}}
  
 
=== Database entries ===
 
=== Database entries ===
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=References=
 
=References=
 
==Localization==
 
==Localization==
<pubmed> 17064365,  20566861 </pubmed>
+
<pubmed> 17064365,  20566861 21636744,21636745 </pubmed>
 
==Other original publications==
 
==Other original publications==
 
<pubmed>19643765,16832063,11290328,12809607,16101995,12530960,7836311,,16950129 9023218, 19659933 19114499, 21091501 20525796</pubmed>
 
<pubmed>19643765,16832063,11290328,12809607,16101995,12530960,7836311,,16950129 9023218, 19659933 19114499, 21091501 20525796</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 05:20, 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 mbl
Synonyms
Essential no
Product MreB-like protein
Function cell shape determination
MW, pI 35 kDa, 5.669
Gene length, protein length 999 bp, 333 aa
Immediate neighbours flhO, spoIIID
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Mbl context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

cell shape, sporulation proteins, membrane proteins

This gene is a member of the following regulons

SigE regulon, stringent response

The gene

Basic information

  • Locus tag: BSU36410

Phenotypes of a mutant

non-viable in the presence of low Mg(2+), readily accumulate rsgI suppressor mutants PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • forms helical filaments in a heterologous system 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, Mbl 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 Mbl PubMed seem to be misinterpretation of data PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • expressed early during sporulation in the mother cell (SigE) PubMed
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • Regulatory mechanism:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Görke lab

Labs working on this gene/protein

Peter Graumann, Freiburg University, Germany homepage

Your additional remarks

References

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