TyrS

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  • Description: tyrosly-tRNA synthetase (major)

Gene name tyrS
Synonyms
Essential yes PubMed
Product tyrosly-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
TyrS context.gif
This image was kindly provided by SubtiList







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)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • 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)