TrmFO

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

translation

The gene

Basic information

• Locus tag: BSU16130

Database entries

• BsubCyc: BSU16130

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Cofactors: FAD, methylene-THF PubMed

• Effectors of protein activity:

• Interactions:

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU16130

• Structure:
  • 3G5S (TrmFO from Thermus thermophilus, 54% identity, 79% similarity) PubMed

• UniProt: P39815

• KEGG entry: [2]

• E.C. number: 2.1.1.74

Expression and regulation

• Operon:

• Expression browser: trmFO PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)