Difference between revisions of "CymR"
(→Categories containing this gene/protein) |
|||
Line 1: | Line 1: | ||
− | * '''Description:''' pleiotropic regulator of | + | * '''Description:''' pleiotropic regulator of [[sulfur metabolism]] <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
Line 12: | Line 12: | ||
|style="background:#ABCDEF;" align="center"| '''Product''' || transcription repressor | |style="background:#ABCDEF;" align="center"| '''Product''' || transcription repressor | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || regulation of | + | |style="background:#ABCDEF;" align="center"|'''Function''' || regulation of [[sulfur metabolism]] |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/riboflavin.html Riboflavin / FAD], [http://subtiwiki.uni-goettingen.de/pathways/cys_meth_and_sulfate_assimilation.html Cys, Met & Sulfate assimilation]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/riboflavin.html Riboflavin / FAD], [http://subtiwiki.uni-goettingen.de/pathways/cys_meth_and_sulfate_assimilation.html Cys, Met & Sulfate assimilation]''' | ||
Line 59: | Line 59: | ||
=== Additional information=== | === Additional information=== | ||
− | |||
− | |||
Line 88: | Line 86: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' [[CymR]]-[[CysK]], the complex is formed in the presence of cysteine, and results in DNA binding and repression of genes of cysteine biosynthesis [http://www.ncbi.nlm.nih.gov/sites/entrez/18974048 PubMed] | + | * '''Interactions:''' |
+ | ** [[CymR]]-[[CysK]], the complex is formed in the presence of cysteine, and results in DNA binding and repression of genes of cysteine biosynthesis [http://www.ncbi.nlm.nih.gov/sites/entrez/18974048 PubMed] | ||
* '''Localization:''' cytoplasm (according to Swiss-Prot) | * '''Localization:''' cytoplasm (according to Swiss-Prot) | ||
Line 94: | Line 93: | ||
=== Database entries === | === Database entries === | ||
− | * '''Structure:''' | + | * '''Structure:''' {{PubMed|21624051}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/O34527 O34527] | * '''UniProt:''' [http://www.uniprot.org/uniprot/O34527 O34527] | ||
Line 140: | Line 139: | ||
<pubmed>16513748, </pubmed> | <pubmed>16513748, </pubmed> | ||
==Other original publications== | ==Other original publications== | ||
− | <pubmed>18974048,17056751,16109943,16885442 11948165 , 15668000 20608979 </pubmed> | + | <pubmed>18974048,17056751,16109943,16885442 11948165 , 15668000 20608979 21624051</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 08:35, 2 June 2011
- Description: pleiotropic regulator of sulfur metabolism
Gene name | cymR |
Synonyms | yrzC |
Essential | no |
Product | transcription repressor |
Function | regulation of sulfur metabolism |
Metabolic function and regulation of this protein in SubtiPathways: Riboflavin / FAD, Cys, Met & Sulfate assimilation | |
MW, pI | 11 kDa, 9.879 |
Gene length, protein length | 333 bp, 111 aa |
Immediate neighbours | yrvO, yrvN |
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
sulfur metabolism, transcription factors and their control, regulators of core metabolism
This gene is a member of the following regulons
The CymR regulon
The gene
Basic information
- Locus tag: BSU27520
Phenotypes of a mutant
- impaired growth in the presence of cystine and increased sensitivity to hydrogen peroxide-, disulfide-, paraquat- and tellurite-induced stresses PubMed
- increased intracellular cysteine pool and hydrogen sulfide formation PubMed
- depletion of branched-chain amino acids PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: Rrf2 family of transcription regulators
- Paralogous protein(s):
Genes repressed by CymR
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure: PubMed
- UniProt: O34527
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Isabelle Martin-Verstraete, Institute Pasteur, Paris, France
Your additional remarks
References
The CymR regulon
Sergine Even, Pierre Burguière, Sandrine Auger, Olga Soutourina, Antoine Danchin, Isabelle Martin-Verstraete
Global control of cysteine metabolism by CymR in Bacillus subtilis.
J Bacteriol: 2006, 188(6);2184-97
[PubMed:16513748]
[WorldCat.org]
[DOI]
(P p)
Other original publications
William Shepard, Olga Soutourina, Emmanuelle Courtois, Patrick England, Ahmed Haouz, Isabelle Martin-Verstraete
Insights into the Rrf2 repressor family--the structure of CymR, the global cysteine regulator of Bacillus subtilis.
FEBS J: 2011, 278(15);2689-701
[PubMed:21624051]
[WorldCat.org]
[DOI]
(I p)
Marie-Françoise Hullo, Isabelle Martin-Verstraete, Olga Soutourina
Complex phenotypes of a mutant inactivated for CymR, the global regulator of cysteine metabolism in Bacillus subtilis.
FEMS Microbiol Lett: 2010, 309(2);201-7
[PubMed:20608979]
[WorldCat.org]
[DOI]
(I p)
Catherine Tanous, Olga Soutourina, Bertrand Raynal, Marie-Françoise Hullo, Peggy Mervelet, Anne-Marie Gilles, Philippe Noirot, Antoine Danchin, Patrick England, Isabelle Martin-Verstraete
The CymR regulator in complex with the enzyme CysK controls cysteine metabolism in Bacillus subtilis.
J Biol Chem: 2008, 283(51);35551-60
[PubMed:18974048]
[WorldCat.org]
[DOI]
(P p)
Marie-Françoise Hullo, Sandrine Auger, Olga Soutourina, Octavian Barzu, Mireille Yvon, Antoine Danchin, Isabelle Martin-Verstraete
Conversion of methionine to cysteine in Bacillus subtilis and its regulation.
J Bacteriol: 2007, 189(1);187-97
[PubMed:17056751]
[WorldCat.org]
[DOI]
(P p)
Soon-Yong Choi, Dindo Reyes, Montira Leelakriangsak, Peter Zuber
The global regulator Spx functions in the control of organosulfur metabolism in Bacillus subtilis.
J Bacteriol: 2006, 188(16);5741-51
[PubMed:16885442]
[WorldCat.org]
[DOI]
(P p)
Pierre Burguière, Juliette Fert, Isabelle Guillouard, Sandrine Auger, Antoine Danchin, Isabelle Martin-Verstraete
Regulation of the Bacillus subtilis ytmI operon, involved in sulfur metabolism.
J Bacteriol: 2005, 187(17);6019-30
[PubMed:16109943]
[WorldCat.org]
[DOI]
(P p)
Irina M Solovieva, Rimma A Kreneva, Lubov Errais Lopes, Daniel A Perumov
The riboflavin kinase encoding gene ribR of Bacillus subtilis is a part of a 10 kb operon, which is negatively regulated by the yrzC gene product.
FEMS Microbiol Lett: 2005, 243(1);51-8
[PubMed:15668000]
[WorldCat.org]
[DOI]
(P p)
Christine Eymann, Georg Homuth, Christian Scharf, Michael Hecker
Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis.
J Bacteriol: 2002, 184(9);2500-20
[PubMed:11948165]
[WorldCat.org]
[DOI]
(P p)