Difference between revisions of "TrmFO"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 458 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 458 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 1069 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 1069 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 237 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 237 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 439 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 15:06, 17 April 2014

  • Description: flavoprotein, tRNA:m(5)U-54 methyltransferase, glucose-inhibited division protein

Gene name trmFO
Synonyms ylyC, gid
Essential no
Product tRNA:m(5)U-54 methyltransferase
Function tRNA modification
Gene expression levels in SubtiExpress: trmFO
MW, pI 47 kDa, 5.767
Gene length, protein length 1305 bp, 435 aa
Immediate neighbours topA, codV
Sequences Protein DNA DNA_with_flanks
Genetic context
Gid context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TrmFO expression.png















Categories containing this gene/protein

translation

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU16130

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: catalyzes the folate-dependent C(5)-methylation of uridine at position 54 in the TpsiC loop of tRNA
  • Protein family: TrmFO subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure:
    • 3G5S (TrmFO from Thermus thermophilus, 54% identity, 79% similarity) PubMed
  • 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): 458 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 1069 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 237 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 237 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 439 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Djemel Hamdane, Eduardo Bruch, Sun Un, Martin Field, Marc Fontecave
Activation of a unique flavin-dependent tRNA-methylating agent.
Biochemistry: 2013, 52(49);8949-56
[PubMed:24228791] [WorldCat.org] [DOI] (I p)

Djemel Hamdane, Manuela Argentini, David Cornu, Béatrice Golinelli-Pimpaneau, Marc Fontecave
FAD/folate-dependent tRNA methyltransferase: flavin as a new methyl-transfer agent.
J Am Chem Soc: 2012, 134(48);19739-45
[PubMed:23157377] [WorldCat.org] [DOI] (I p)

Ryota Yamagami, Koki Yamashita, Hiroshi Nishimasu, Chie Tomikawa, Anna Ochi, Chikako Iwashita, Akira Hirata, Ryuichiro Ishitani, Osamu Nureki, Hiroyuki Hori
The tRNA recognition mechanism of folate/FAD-dependent tRNA methyltransferase (TrmFO).
J Biol Chem: 2012, 287(51);42480-94
[PubMed:23095745] [WorldCat.org] [DOI] (I p)

Djemel Hamdane, Manuela Argentini, David Cornu, Hannu Myllykallio, Stéphane Skouloubris, Gaston Hui-Bon-Hoa, Béatrice Golinelli-Pimpaneau
Insights into folate/FAD-dependent tRNA methyltransferase mechanism: role of two highly conserved cysteines in catalysis.
J Biol Chem: 2011, 286(42);36268-80
[PubMed:21846722] [WorldCat.org] [DOI] (I p)

Djemel Hamdane, Vincent Guerineau, Sun Un, Beatrice Golinelli-Pimpaneau
A catalytic intermediate and several flavin redox states stabilized by folate-dependent tRNA methyltransferase from Bacillus subtilis.
Biochemistry: 2011, 50(23);5208-19
[PubMed:21561081] [WorldCat.org] [DOI] (I p)

Djemel Hamdane, Stéphane Skouloubris, Hannu Myllykallio, Béatrice Golinelli-Pimpaneau
Expression and purification of untagged and histidine-tagged folate-dependent tRNA:m5U54 methyltransferase from Bacillus subtilis.
Protein Expr Purif: 2010, 73(1);83-9
[PubMed:20412857] [WorldCat.org] [DOI] (I p)

Hiroshi Nishimasu, Ryuichiro Ishitani, Koki Yamashita, Chikako Iwashita, Akira Hirata, Hiroyuki Hori, Osamu Nureki
Atomic structure of a folate/FAD-dependent tRNA T54 methyltransferase.
Proc Natl Acad Sci U S A: 2009, 106(20);8180-5
[PubMed:19416846] [WorldCat.org] [DOI] (I p)

Jaunius Urbonavicius, Stéphane Skouloubris, Hannu Myllykallio, Henri Grosjean
Identification of a novel gene encoding a flavin-dependent tRNA:m5U methyltransferase in bacteria--evolutionary implications.
Nucleic Acids Res: 2005, 33(13);3955-64
[PubMed:16027442] [WorldCat.org] [DOI] (I e)