Difference between revisions of "GlyQ"

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(Expression and regulation)
(Database entries)
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:'''
+
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1J5W 1J5W] (from ''Thermotoga maritima'', 55% identity, 72% similarity)
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P54380 P54380]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P54380 P54380]

Revision as of 16:50, 18 February 2010

  • Description: glycyl-tRNA synthetase (alpha subunit)

Gene name glyQ
Synonyms yqfJ
Essential yes PubMed
Product glycyl-tRNA synthetase (alpha subunit)
Function translation
Metabolic function and regulation of this protein in SubtiPathways:
tRNA charging
MW, pI 33 kDa, 4.8
Gene length, protein length 885 bp, 295 aa
Immediate neighbours glyS, recO
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
GlyQ context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU25270

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: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly) (according to Swiss-Prot)
  • Protein family: class-II aminoacyl-tRNA synthetase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure: 1J5W (from Thermotoga maritima, 55% identity, 72% similarity)
  • KEGG entry: [3]

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)

Audrey R Nelson, Tina M Henkin, Paul F Agris
tRNA regulation of gene expression: interactions of an mRNA 5'-UTR with a regulatory tRNA.
RNA: 2006, 12(7);1254-61
[PubMed:16741230] [WorldCat.org] [DOI] (P p)

Mary R Yousef, Frank J Grundy, Tina M Henkin
Structural transitions induced by the interaction between tRNA(Gly) and the Bacillus subtilis glyQS T box leader RNA.
J Mol Biol: 2005, 349(2);273-87
[PubMed:15890195] [WorldCat.org] [DOI] (P p)

Frank J Grundy, Mary R Yousef, Tina M Henkin
Monitoring uncharged tRNA during transcription of the Bacillus subtilis glyQS gene.
J Mol Biol: 2005, 346(1);73-81
[PubMed:15663928] [WorldCat.org] [DOI] (P p)

Frank J Grundy, Tina M Henkin
Kinetic analysis of tRNA-directed transcription antitermination of the Bacillus subtilis glyQS gene in vitro.
J Bacteriol: 2004, 186(16);5392-9
[PubMed:15292140] [WorldCat.org] [DOI] (P p)

Mary R Yousef, Frank J Grundy, Tina M Henkin
tRNA requirements for glyQS antitermination: a new twist on tRNA.
RNA: 2003, 9(9);1148-56
[PubMed:12923262] [WorldCat.org] [DOI] (P p)