Difference between revisions of "TyrS"
Line 37: | Line 37: | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
− | + | <br/><br/> | |
− | |||
− | |||
− | |||
− | |||
= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
Line 99: | Line 95: | ||
=== Database entries === | === Database entries === | ||
− | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId= | + | * '''Structure:''' |
+ | ** [http://www.rcsb.org/pdb/explore.do?structureId=1JH3 1JH3] (C-terminal domain, Geobacillus stearothermophilus) | ||
+ | ** [http://www.rcsb.org/pdb/explore.do?structureId=3TS1 3TS1] (complex with tyrosyl adenylate intermediate, Geobacillus stearothermophilus) | ||
+ | ** [http://www.rcsb.org/pdb/explore.do?structureId=1N53 1N53] (the [[T-box]] antiterminator RNA) [http://www.ncbi.nlm.nih.gov/sites/entrez/12547201 PubMed] | ||
* '''UniProt:''' [http://www.uniprot.org/uniprot/P22326 P22326] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P22326 P22326] |
Revision as of 14:34, 12 July 2013
- Description: tyrosyl-tRNA synthetase (major)
Gene name | tyrS |
Synonyms | |
Essential | yes PubMed |
Product | tyrosyl-tRNA synthetase (major) |
Function | translation |
Gene expression levels in SubtiExpress: tyrS | |
Metabolic function and regulation of this protein in SubtiPathways: tRNA charging | |
MW, pI | 47 kDa, 5.213 |
Gene length, protein length | 1266 bp, 422 aa |
Immediate neighbours | rpsD, ytzK |
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: 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:
Database entries
- Structure:
- UniProt: P22326
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- T-box: RNA switch, transcriptional antitermination PubMed
- 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
Reviews
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)
M Pelchat, J Lapointe
Aminoacyl-tRNA synthetase genes of Bacillus subtilis: organization and regulation.
Biochem Cell Biol: 1999, 77(4);343-7
[PubMed:10546897]
[WorldCat.org]
(P p)
Original publications
Jiachen Wang, Edward P Nikonowicz
Solution structure of the K-turn and Specifier Loop domains from the Bacillus subtilis tyrS T-box leader RNA.
J Mol Biol: 2011, 408(1);99-117
[PubMed:21333656]
[WorldCat.org]
[DOI]
(I p)
Jiachen Wang, Tina M Henkin, Edward P Nikonowicz
NMR structure and dynamics of the Specifier Loop domain from the Bacillus subtilis tyrS T box leader RNA.
Nucleic Acids Res: 2010, 38(10);3388-98
[PubMed:20110252]
[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)