Difference between revisions of "MreB"
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− | * '''Description:''' cell- | + | * '''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] | ||
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− | |style="background:#ABCDEF;" align="center"| '''Product''' || cell- | + | |style="background:#ABCDEF;" align="center"| '''Product''' || [[cell shape]]-determining protein |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || cell | + | |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 === | ||
− | + | * 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] |
=== Database entries === | === Database entries === | ||
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=== Additional information=== | === Additional information=== | ||
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− | |||
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' [[MreB]]-[[TufA]] {{PubMed|20133608}} | + | * '''[[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 | + | ** during logarithmic growth, [[MreB]] forms discrete patches thst move processively along peripheral tracks perpendicular to the cell axis {{PubMed|21636744}} |
− | ** | + | ** 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 This image was kindly provided by SubtiList
|
Contents
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
The gene
Basic information
- Locus tag: BSU28030
Phenotypes of a mutant
- essential PubMed
- the mutation can be suppressed by inactivation of ponA, ptsI, ccpA PubMed, by overexpression of YvcK PubMed, or by addition of 5 mM magnesium to the growth medium PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- 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
- UniProt: Q01465
- 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:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in the labs of Jeff Errington and Boris Görke
- Antibody: available in the Jeff Errington and Peter Graumann labs
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