Tgt

From SubtiWiki
Revision as of 09:48, 17 April 2014 by 134.76.70.252 (talk)
Jump to: navigation, search
  • Description: tRNA-guanine transglycosylase

Gene name tgt
Synonyms
Essential no
Product tRNA-guanine transglycosylase
Function tRNA modification
Gene expression levels in SubtiExpress: tgt
MW, pI 43 kDa, 6.149
Gene length, protein length 1143 bp, 381 aa
Immediate neighbours yrbF, queA
Sequences Protein DNA DNA_with_flanks
Genetic context
Tgt context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Tgt expression.png
























Categories containing this gene/protein

translation, membrane proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU27710

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: [tRNA]-guanine + queuine = [tRNA]-queuine + guanine (according to Swiss-Prot)
  • Protein family: queuine tRNA-ribosyltransferase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 258 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 1005 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Ruth Brenk, Milton T Stubbs, Andreas Heine, Klaus Reuter, Gerhard Klebe
Flexible adaptations in the structure of the tRNA-modifying enzyme tRNA-guanine transglycosylase and their implications for substrate selectivity, reaction mechanism and structure-based drug design.
Chembiochem: 2003, 4(10);1066-77
[PubMed:14523925] [WorldCat.org] [DOI] (P p)

Wei Xie, Xianjun Liu, Raven H Huang
Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate.
Nat Struct Biol: 2003, 10(10);781-8
[PubMed:12949492] [WorldCat.org] [DOI] (P p)

DeeAnne M Goodenough-Lashua, George A Garcia
tRNA-guanine transglycosylase from E. coli: a ping-pong kinetic mechanism is consistent with nucleophilic catalysis.
Bioorg Chem: 2003, 31(4);331-44
[PubMed:12877882] [WorldCat.org] [DOI] (P p)

G A Garcia, D L Tierney, S Chong, K Clark, J E Penner-Hahn
X-ray absorption spectroscopy of the zinc site in tRNA-guanine transglycosylase from Escherichia coli.
Biochemistry: 1996, 35(9);3133-9
[PubMed:8608154] [WorldCat.org] [DOI] (P p)

A W Curnow, G A Garcia
tRNA-guanine transglycosylase from Escherichia coli. Minimal tRNA structure and sequence requirements for recognition.
J Biol Chem: 1995, 270(29);17264-7
[PubMed:7615526] [WorldCat.org] [DOI] (P p)

S Chong, A W Curnow, T J Huston, G A Garcia
tRNA-guanine transglycosylase from Escherichia coli is a zinc metalloprotein. Site-directed mutagenesis studies to identify the zinc ligands.
Biochemistry: 1995, 34(11);3694-701
[PubMed:7893665] [WorldCat.org] [DOI] (P p)

S O Mueller, R K Slany
Structural analysis of the interaction of the tRNA modifying enzymes Tgt and QueA with a substrate tRNA.
FEBS Lett: 1995, 361(2-3);259-64
[PubMed:7698334] [WorldCat.org] [DOI] (P p)

A W Curnow, F L Kung, K A Koch, G A Garcia
tRNA-guanine transglycosylase from Escherichia coli: gross tRNA structural requirements for recognition.
Biochemistry: 1993, 32(19);5239-46
[PubMed:8494901] [WorldCat.org] [DOI] (P p)

S Noguchi, Y Nishimura, Y Hirota, S Nishimura
Isolation and characterization of an Escherichia coli mutant lacking tRNA-guanine transglycosylase. Function and biosynthesis of queuosine in tRNA.
J Biol Chem: 1982, 257(11);6544-50
[PubMed:6804468] [WorldCat.org] (P p)