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  
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"| '''Product''' || MreB-like protein
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|style="background:#ABCDEF;" align="center"| '''Product''' || [[MreB]]-like protein
 
|-
 
|-
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|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:'''
  
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* '''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}}
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** [[Mbl]]-[[MreBH]] [http://www.ncbi.nlm.nih.gov/sites/entrez/17064365 PubMed]
  
 
* '''Localization:'''  
 
* '''Localization:'''  
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** 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}}
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** 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]
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** 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==
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<pubmed> 17064365,  20566861 </pubmed>
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<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

Hervé Joël Defeu Soufo, Peter L Graumann
Bacillus subtilis MreB paralogues have different filament architectures and lead to shape remodelling of a heterologous cell system.
Mol Microbiol: 2010, 78(5);1145-58
[PubMed:21091501] [WorldCat.org] [DOI] (I p)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Yoshikazu Kawai, Kei Asai, Jeffery Errington
Partial functional redundancy of MreB isoforms, MreB, Mbl and MreBH, in cell morphogenesis of Bacillus subtilis.
Mol Microbiol: 2009, 73(4);719-31
[PubMed:19659933] [WorldCat.org] [DOI] (I p)

Kathrin Schirner, Jeff Errington
Influence of heterologous MreB proteins on cell morphology of Bacillus subtilis.
Microbiology (Reading): 2009, 155(Pt 11);3611-3621
[PubMed:19643765] [WorldCat.org] [DOI] (I p)

Kathrin Schirner, Jeff Errington
The cell wall regulator {sigma}I specifically suppresses the lethal phenotype of mbl mutants in Bacillus subtilis.
J Bacteriol: 2009, 191(5);1404-13
[PubMed:19114499] [WorldCat.org] [DOI] (I p)

Rut Carballido-López, Alex Formstone, Ying Li, S Dusko Ehrlich, Philippe Noirot, Jeff Errington
Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE.
Dev Cell: 2006, 11(3);399-409
[PubMed:16950129] [WorldCat.org] [DOI] (P p)

Kittichoat Tiyanont, Thierry Doan, Michael B Lazarus, Xiao Fang, David Z Rudner, Suzanne Walker
Imaging peptidoglycan biosynthesis in Bacillus subtilis with fluorescent antibiotics.
Proc Natl Acad Sci U S A: 2006, 103(29);11033-8
[PubMed:16832063] [WorldCat.org] [DOI] (P p)

Mark Leaver, Jeff Errington
Roles for MreC and MreD proteins in helical growth of the cylindrical cell wall in Bacillus subtilis.
Mol Microbiol: 2005, 57(5);1196-209
[PubMed:16101995] [WorldCat.org] [DOI] (P p)

Richard A Daniel, Jeff Errington
Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell.
Cell: 2003, 113(6);767-76
[PubMed:12809607] [WorldCat.org] [DOI] (P p)

Rut Carballido-López, Jeff Errington
The bacterial cytoskeleton: in vivo dynamics of the actin-like protein Mbl of Bacillus subtilis.
Dev Cell: 2003, 4(1);19-28
[PubMed:12530960] [WorldCat.org] [DOI] (P p)

L J Jones, R Carballido-López, J Errington
Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis.
Cell: 2001, 104(6);913-22
[PubMed:11290328] [WorldCat.org] [DOI] (P p)

A Decatur, M T McMurry, B N Kunkel, R Losick
Translation of the mRNA for the sporulation gene spoIIID of Bacillus subtilis is dependent upon translation of a small upstream open reading frame.
J Bacteriol: 1997, 179(4);1324-8
[PubMed:9023218] [WorldCat.org] [DOI] (P p)

Y Abhayawardhane, G C Stewart
Bacillus subtilis possesses a second determinant with extensive sequence similarity to the Escherichia coli mreB morphogene.
J Bacteriol: 1995, 177(3);765-73
[PubMed:7836311] [WorldCat.org] [DOI] (P p)

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