Difference between revisions of "TyrZ"

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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1239 bp, 413 aa  
 
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1239 bp, 413 aa  
 
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|-
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ywaE]]'', ''[[ywaD]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[dtrR]]'', ''[[ywaD]]''
 
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|-
 
|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU38460 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU38460 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU38460 DNA_with_flanks]
 
|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU38460 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU38460 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU38460 DNA_with_flanks]

Revision as of 13:30, 4 March 2015

  • Description: alternative tyrosyl-tRNA synthetase, required to prevent misincorporation of D-Tyr into proteins

Gene name tyrZ
Synonyms ipa-9r, tyrS1, tyrT
Essential no
Product tyrosyl-tRNA synthetase (minor)
Function translation
Gene expression levels in SubtiExpress: tyrZ
Metabolic function and regulation of this protein in SubtiPathways:
tyrZ
MW, pI 46 kDa, 6.661
Gene length, protein length 1239 bp, 413 aa
Immediate neighbours dtrR, ywaD
Sequences Protein DNA DNA_with_flanks
Genetic context
TyrZ context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TyrZ expression.png















Categories containing this gene/protein

translation

This gene is a member of the following regulons

DtrR regulon, T-box

The gene

Basic information

  • Locus tag: BSU38460

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr) (according to Swiss-Prot) ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr) (according to Swiss-Prot)
    • TyrZ is highly specific for L-Tyr, prevents misincorporation of D-Tyr into proteins, less processive than TyrS PubMed
  • Protein family: TyrS type 2 subfamily (according to Swiss-Prot), class-I aminoacyl-tRNA synthetase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylated on Thr-311 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Additional information:

Biological materials

  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

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)

Boumediene Soufi, Chanchal Kumar, Florian Gnad, Matthias Mann, Ivan Mijakovic, Boris Macek
Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis.
J Proteome Res: 2010, 9(7);3638-46
[PubMed:20509597] [WorldCat.org] [DOI] (I p)

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)

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)