TyrS

• 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: tyrS
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

Categories containing this gene/protein

translation, essential genes, most abundant proteins

This gene is a member of the following regulons

T-box

The gene

Basic information

• Locus tag: BSU29670

Phenotypes of a mutant

• essential PubMed
• the gene can be deleted, but the mutant acquires suppressors in dtrR to allow expression of tyrZ PubMed
• a tyrS tyrZ double mutant is not viable PubMed

Database entries

• BsubCyc: BSU29670

• 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:

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU29670

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

• UniProt: P22326

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: tyrS PubMed

• Expression browser: 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:
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 848 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 3406 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4314 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1369 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1521 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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

Sara A Leiman, Charles Richardson, Lucy Foulston, Alexander K W Elsholz, Eric A First, Richard Losick
Identification and characterization of mutations conferring resistance to D-amino acids in Bacillus subtilis.
J Bacteriol: 2015, 197(9);1632-9
[PubMed:25733611] [WorldCat.org] [DOI] (I p)

Rebecca N Williams-Wagner, Frank J Grundy, Medha Raina, Michael Ibba, Tina M Henkin
The Bacillus subtilis tyrZ gene encodes a highly selective tyrosyl-tRNA synthetase and is regulated by a MarR regulator and T box riboswitch.
J Bacteriol: 2015, 197(9);1624-31
[PubMed:25733610] [WorldCat.org] [DOI] (I p)

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)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P 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)