Difference between revisions of "GlyQ"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 821 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 821 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 1704 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 1704 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1622 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1214 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1611 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 14:07, 17 April 2014

  • Description: glycyl-tRNA synthetase (alpha subunit)

Gene name glyQ
Synonyms yqfJ
Essential yes PubMed
Product glycyl-tRNA synthetase (alpha subunit)
Function translation
Gene expression levels in SubtiExpress: glyQ
Interactions involving this protein in SubtInteract: GlyQ
Metabolic function and regulation of this protein in SubtiPathways:
glyQ
MW, pI 33 kDa, 4.8
Gene length, protein length 885 bp, 295 aa
Immediate neighbours glyS, recO
Sequences Protein DNA DNA_with_flanks
Genetic context
GlyQ context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
GlyQ 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: 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:
  • Modification:
  • Effectors of protein activity:

Database entries

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

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): 821 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 1704 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1622 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1214 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1611 PubMed

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)

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)

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)