Difference between revisions of "TyrS"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:''' [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], [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)
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* '''Structure:'''  
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** [http://www.rcsb.org/pdb/explore.do?structureId=1JH3 1JH3] (C-terminal domain, Geobacillus stearothermophilus)  
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** [http://www.rcsb.org/pdb/explore.do?structureId=3TS1 3TS1] (complex with tyrosyl adenylate intermediate, Geobacillus stearothermophilus)
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** [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
TyrS context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TyrS expression.png















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]

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:
    • 1JH3 (C-terminal domain, Geobacillus stearothermophilus)
    • 3TS1 (complex with tyrosyl adenylate intermediate, Geobacillus stearothermophilus)
    • 1N53 (the T-box antiterminator RNA) PubMed
  • 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

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)