Difference between revisions of "MutY"
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* '''Additional information:''' | * '''Additional information:''' | ||
** number of protein molecules per cell (minimal medium with glucose and ammonium): 52 {{PubMed|24696501}} | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 52 {{PubMed|24696501}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 168 {{PubMed|21395229}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 201 {{PubMed|21395229}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 215 {{PubMed|21395229}} | ||
=Biological materials = | =Biological materials = | ||
− | |||
* '''Mutant:''' | * '''Mutant:''' | ||
Revision as of 14:17, 17 April 2014
- Description: A/G-specific adenine glycosylase, error prevention oxidized guanine system, releases adenines from 8-oxo-G:A mismatches
Gene name | mutY |
Synonyms | yfhQ |
Essential | no |
Product | A/G-specific adenine glycosylase |
Function | DNA repair |
Gene expression levels in SubtiExpress: mutY | |
Metabolic function and regulation of this protein in SubtiPathways: mutY | |
MW, pI | 41 kDa, 6.044 |
Gene length, protein length | 1107 bp, 369 aa |
Immediate neighbours | yfhP, yfhS |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU08630
Phenotypes of a mutant
Database entries
- BsubCyc: BSU08630
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: releases adenines from 8-oxo-G:A mismatches
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- BsubCyc: BSU08630
- Structure: 1RRS (complex with DNA, Geobacillus stearothermophilus)
- UniProt: O31584
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
- number of protein molecules per cell (minimal medium with glucose and ammonium): 52 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 168 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 201 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 215 PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Justin S Lenhart, Jeremy W Schroeder, Brian W Walsh, Lyle A Simmons
DNA repair and genome maintenance in Bacillus subtilis.
Microbiol Mol Biol Rev: 2012, 76(3);530-64
[PubMed:22933559]
[WorldCat.org]
[DOI]
(I p)
Original publications
Bernardo N Debora, Luz E Vidales, Rosario Ramírez, Mariana Ramírez, Eduardo A Robleto, Ronald E Yasbin, Mario Pedraza-Reyes
Mismatch repair modulation of MutY activity drives Bacillus subtilis stationary-phase mutagenesis.
J Bacteriol: 2011, 193(1);236-45
[PubMed:20971907]
[WorldCat.org]
[DOI]
(I p)
Luz E Vidales, Lluvia C Cárdenas, Eduardo Robleto, Ronald E Yasbin, Mario Pedraza-Reyes
Defects in the error prevention oxidized guanine system potentiate stationary-phase mutagenesis in Bacillus subtilis.
J Bacteriol: 2009, 191(2);506-13
[PubMed:19011023]
[WorldCat.org]
[DOI]
(I p)
Hiroki Yamamoto, Masao Mori, Junichi Sekiguchi
Transcription of genes near the sspE locus of the Bacillus subtilis genome.
Microbiology (Reading): 1999, 145 ( Pt 8);2171-2180
[PubMed:10463184]
[WorldCat.org]
[DOI]
(P p)