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InterPro: IPR002649 tRNA (guanine-N1-)-methyltransferase, bacteria

Protein matchesHelp
UniProtKB
Matches:
1627 proteins
AccessionHelp IPR002649 tRNA_m1G_MeTrfase_bac
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR016009 tRNA (guanine-N1-)-methyltransferase
GO Term annotationHelp
Process GO:0008033 tRNA processing
Function GO:0003723 RNA binding
GO:0009019 tRNA (guanine-N1-)-methyltransferase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

In transfer RNA many different modified nucleosides are found, especially in the anticodon region. tRNA (guanine-N1-)-methyltransferase EC:2.1.1.31 is one of several nucleases operating together with the tRNA-modifying enzymes before the formation of the mature tRNA. It catalyses the reaction:

S-adenosyl-L-methionine + tRNA -> S-adenosyl-L-homocysteine + tRNA containing N1-methylguanine

methylating guanosine(G) to N1-methylguanine (1-methylguanosine (m1G)) at position 37 of tRNAs that read CUN (leucine), CCN(proline), and CGG (arginine) codons. The presence of m1G improves the cellular growth rate and the polypeptide steptime and also prevents the tRNA from shifting the reading frame [1].

The mechanism of the trmD3-induced frameshift involving mutant tRNA(Pro) and tRNA(Leu) species has been investigated [2]. It has been suggested that the conformation of the anticodon loop may be a major determining element for the formation of m1G37 in vivo [3].

Structural linksHelp
SCOP: c.116.1.4
Database linksHelp
Enzyme: EC:2.1.1.31
Blocks: IPB002649

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR002649 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
A5GMI5 tRNA (guanine-N(1)-)-methyltransferase

O67463 tRNA (guanine-N(1)-)-methyltransferase

P72828 tRNA (guanine-N(1)-)-methyltransferase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR002649 tRNA (guanine-N1-)-methyltransferase, bacteria
IPR016009 tRNA (guanine-N1-)-methyltransferase
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
1. Hagervall TG, Ericson JU, Esberg KB, Li JN, Bjork GR.
Role of tRNA modification in translational fidelity.
Biochim. Biophys. Acta 1050 263-6 1990 [PubMed: 2207153]
http://dx.doi.org/10.1016/0167-4781(90)90178-5
2. Hagervall TG, Tuohy TM, Atkins JF, Bjork GR.
Deficiency of 1-methylguanosine in tRNA from Salmonella typhimurium induces frameshifting by quadruplet translocation.
J. Mol. Biol. 232 756-65 1993 [PubMed: 7689113]
http://dx.doi.org/10.1006/jmbi.1993.1429
3. Qian Q, Bjork GR.
Structural requirements for the formation of 1-methylguanosine in vivo in tRNA(Pro)GGG of Salmonella typhimurium.
J. Mol. Biol. 266 283-96 1997 [PubMed: 9047363]
http://dx.doi.org/10.1006/jmbi.1996.0789

Additional ReadingHelp
Hjalmarsson KJ, Bystrom AS, Bjork GR.
Purification and characterization of transfer RNA (guanine-1)methyltransferase from Escherichia coli.
J. Biol. Chem. 258 1983 1343-51 [PubMed: 6337136]
http://intl.jbc.org/cgi/reprint/258/2/1343.pdf
Elkins PA, Watts JM, Zalacain M, van Thiel A, Vitazka PR, Redlak M, Andraos-Selim C, Rastinejad F, Holmes WM.
Insights into catalysis by a knotted TrmD tRNA methyltransferase.
J. Mol. Biol. 333 2003 931-49 [PubMed: 14583191]
http://dx.doi.org/10.1016/j.jmb.2003.09.011
O'Dwyer K, Watts JM, Biswas S, Ambrad J, Barber M, Brule H, Petit C, Holmes DJ, Zalacain M, Holmes WM.
Characterization of Streptococcus pneumoniae TrmD, a tRNA methyltransferase essential for growth.
J. Bacteriol. 186 2004 2346-54 [PubMed: 15060037]
http://dx.doi.org/10.1128/JB.186.8.2346-2354.2004
Liu J, Wang W, Shin DH, Yokota H, Kim R, Kim SH.
Crystal structure of tRNA (m1G37) methyltransferase from Aquifex aeolicus at 2.6 A resolution: a novel methyltransferase fold.
Proteins 53 2003 326-8 [PubMed: 14517984]
http://dx.doi.org/10.1002/prot.10479
Ahn HJ, Kim HW, Yoon HJ, Lee BI, Suh SW, Yang JK.
Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition.
EMBO J. 22 2003 2593-603 [PubMed: 12773376]
http://dx.doi.org/10.1093/emboj/cdg269
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InterPro 23.1