TyrS

• Description: tyrosyl-tRNA synthetase (major)
  
  

Gene name	tyrS
Synonyms
Essential	yes PubMed
Product	tyrosyl-tRNA synthetase (major)
Function	translation
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, acsA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

translation, essential genes

This gene is a member of the following regulons

T-box

The gene

Basic information

• Locus tag: BSU29670

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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)

• UniProt: P22326

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: tyrS PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by tyrosine limitation (T-box) PubMed

• Regulatory mechanism:
  • T-box: RNA switch, transcriptional antitermination PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original publications

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)