Difference between revisions of "TyrS"
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Revision as of 19:56, 15 June 2009
- Description: tyrosly-tRNA synthetase (major)
Gene name | tyrS |
Synonyms | |
Essential | yes PubMed |
Product | tyrosly-tRNA synthetase (major) |
Function | translation |
MW, pI | 47 kDa, 5.213 |
Gene length, protein length | 1266 bp, 422 aa |
Immediate neighbours | rpsD, acsA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU29670
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 1N53 (the T-box antiterminator RNA) PubMed, 1JH3 (C-terminal domain, Geobacillus stearothermophilus), 3TS1 (complex with tyrosyl adenylate intermediate, Geobacillus stearothermophilus)
- Swiss prot entry:
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Ana Gutiérrez-Preciado, Tina M Henkin, Frank J Grundy, Charles Yanofsky, Enrique Merino
Biochemical features and functional implications of the RNA-based T-box regulatory mechanism.
Microbiol Mol Biol Rev: 2009, 73(1);36-61
[PubMed:19258532]
[WorldCat.org]
[DOI]
(I p)
Melinda S Gerdeman, Tina M Henkin, Jennifer V Hines
Solution structure of the Bacillus subtilis T-box antiterminator RNA: seven nucleotide bulge characterized by stacking and flexibility.
J Mol Biol: 2003, 326(1);189-201
[PubMed:12547201]
[WorldCat.org]
[DOI]
(P p)
Melinda S Gerdeman, Tina M Henkin, Jennifer V Hines
In vitro structure-function studies of the Bacillus subtilis tyrS mRNA antiterminator: evidence for factor-independent tRNA acceptor stem binding specificity.
Nucleic Acids Res: 2002, 30(4);1065-72
[PubMed:11842119]
[WorldCat.org]
[DOI]
(I p)
F J Grundy, J A Collins, S M Rollins, T M Henkin
tRNA determinants for transcription antitermination of the Bacillus subtilis tyrS gene.
RNA: 2000, 6(8);1131-41
[PubMed:10943892]
[WorldCat.org]
[DOI]
(P p)
S M Rollins, F J Grundy, T M Henkin
Analysis of cis-acting sequence and structural elements required for antitermination of the Bacillus subtilis tyrS gene.
Mol Microbiol: 1997, 25(2);411-21
[PubMed:9282752]
[WorldCat.org]
[DOI]
(P p)
F J Grundy, S E Hodil, S M Rollins, T M Henkin
Specificity of tRNA-mRNA interactions in Bacillus subtilis tyrS antitermination.
J Bacteriol: 1997, 179(8);2587-94
[PubMed:9098057]
[WorldCat.org]
[DOI]
(P p)
F J Grundy, S M Rollins, T M Henkin
Interaction between the acceptor end of tRNA and the T box stimulates antitermination in the Bacillus subtilis tyrS gene: a new role for the discriminator base.
J Bacteriol: 1994, 176(15);4518-26
[PubMed:8045882]
[WorldCat.org]
[DOI]
(P p)
F J Grundy, T M Henkin
Conservation of a transcription antitermination mechanism in aminoacyl-tRNA synthetase and amino acid biosynthesis genes in gram-positive bacteria.
J Mol Biol: 1994, 235(2);798-804
[PubMed:8289305]
[WorldCat.org]
[DOI]
(P p)
F J Grundy, T M Henkin
tRNA as a positive regulator of transcription antitermination in B. subtilis.
Cell: 1993, 74(3);475-82
[PubMed:8348614]
[WorldCat.org]
[DOI]
(P p)
T M Henkin, B L Glass, F J Grundy
Analysis of the Bacillus subtilis tyrS gene: conservation of a regulatory sequence in multiple tRNA synthetase genes.
J Bacteriol: 1992, 174(4);1299-306
[PubMed:1735721]
[WorldCat.org]
[DOI]
(P p)