Difference between revisions of "TyrS"

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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
 
+
* essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
+
* the gene can be deleted, but the mutant acquires suppressors in ''[[dtrR]]'' to allow expression of ''[[tyrZ]]'' {{PubMed|25733610}}
 +
* a ''[[tyrS]] [[tyrZ]]'' double mutant is not viable {{PubMed|25733610}}
  
 
=== Database entries ===
 
=== Database entries ===
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<pubmed>19258532,10546897 </pubmed>
 
<pubmed>19258532,10546897 </pubmed>
 
==Original publications==
 
==Original publications==
<pubmed>9098057,12547201,11842119,10943892,9282752,8045882,8348614,1735721,8289305,20110252 , 21333656 15378759</pubmed>
+
<pubmed>9098057,12547201,11842119,10943892,9282752,8045882,8348614,1735721,8289305,20110252 , 21333656 15378759 25733610</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 13:11, 4 March 2015

  • 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
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, 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

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:
  • Modification:
  • 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:
    • 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:

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

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)