mRNA (guanine-N7-)-methyltransferase

mRNA (guanine-N7-)-methyltransferase
Identifiers
EC number 2.1.1.56
CAS number 56941-25-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
RNMT
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRNMT, MET, RG7MT1, hCMT1c, CMT1, CMT1c, cm1p, hCMT1, hMet, MRNA-methyltransferase, RNA guanine-7 methyltransferase
External IDsMGI: 1915147 HomoloGene: 2816 GeneCards: RNMT
Gene location (Human)
Chr.Chromosome 18 (human)[1]
Band18p11.21Start13,726,660 bp[1]
End13,764,558 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

8731

67897

Ensembl

ENSG00000101654

ENSMUSG00000009535

UniProt

O43148

Q9D0L8

RefSeq (mRNA)

NM_001308263
NM_003799

NM_001170953
NM_026440
NM_001361002
NM_001361003

RefSeq (protein)

NP_001295192
NP_003790

NP_001164424
NP_080716
NP_001347931
NP_001347932

Location (UCSC)Chr 18: 13.73 – 13.76 MbChr 18: 68.3 – 68.32 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

In enzymology, a mRNA (guanine-N7-)-methyltransferase also known as mRNA cap guanine-N7 methyltransferase is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + G(5')pppR-RNA S-adenosyl-L-homocysteine + m7G(5')pppR-RNA (mRNA containing an N7-methylguanine cap)

Thus, the two substrates of this enzyme are S-adenosyl methionine and G(5')pppR-RNA, whereas its two products are S-adenosylhomocysteine and m7G(5')pppR-RNA. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases.

In humans, mRNA cap guanine-N7 methyltransferase is encoded by the RNMT gene.[5][6][7]

Nomenclature

The systematic name of this enzyme class is S-adenosyl-L-methionine:mRNA (guanine-N7-)-methyltransferase. Other names in common use include:

  • messenger ribonucleate guanine 7-methyltransferase,
  • guanine-7-methyltransferase,
  • messenger RNA guanine 7-methyltransferase, and
  • S-adenosyl-L-methionine:mRNA (guanine-7-N-)-methyltransferase.
  • cap MTase

See also

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000101654 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000009535 - Ensembl, May 2017
  3. "Human PubMed Reference:".
  4. "Mouse PubMed Reference:".
  5. Pillutla RC, Shimamoto A, Furuichi Y, Shatkin AJ (Jan 1999). "Human mRNA capping enzyme (RNGTT) and cap methyltransferase (RNMT) map to 6q16 and 18p11.22-p11.23, respectively". Genomics. 54 (2): 351–3. doi:10.1006/geno.1998.5604. PMID 9828141.
  6. Pillutla RC, Yue Z, Maldonado E, Shatkin AJ (Sep 1998). "Recombinant human mRNA cap methyltransferase binds capping enzyme/RNA polymerase IIo complexes". J Biol Chem. 273 (34): 21443–6. doi:10.1074/jbc.273.34.21443. PMID 9705270.
  7. "Entrez Gene: RNMT RNA (guanine-7-) methyltransferase".

Further reading

  • Ensinger MJ, Martin SA, Paoletti E, Moss B (1975). "Modification of the 5'-terminus of mRNA by soluble guanylyl and methyl transferases from vaccinia virus". Proc. Natl. Acad. Sci. U.S.A. 72 (7): 2525&ndash, 9. doi:10.1073/pnas.72.7.2525. PMC 432801. PMID 1058472.
  • Groner Y, Gilboa E, Aviv H (1978). "Methylation and capping of RNA polymerase II primary transcripts by HeLa nuclear homogenates". Biochemistry. 17 (6): 977&ndash, 82. doi:10.1021/bi00599a005. PMID 629955.
  • Martin SA, Moss B (1975). "Modification of RNA by mRNA guanylyltransferase and mRNA (guanine-7-)methyltransferase from vaccinia virions". J. Biol. Chem. 250 (24): 9330&ndash, 5. PMID 1194287.
  • Martin SA, Paoletti E, Moss B (1975). "Purification of mRNA guanylyltransferase and mRNA (guanine-7-) methyltransferase from vaccinia virions". J. Biol. Chem. 250 (24): 9322&ndash, 9. PMID 1194286.
  • Langberg SR, Moss B (1981). "Post-transcriptional modifications of mRNA. Purification and characterization of cap I and cap II RNA (nucleoside-2'-)-methyltransferases from HeLa cells". J. Biol. Chem. 256 (19): 10054–60. PMID 7275966.
  • Ishikawa K, Nagase T, Nakajima D, et al. (1998). "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 4 (5): 307–13. doi:10.1093/dnares/4.5.307. PMID 9455477.
  • Tsukamoto T, Shibagaki Y, Niikura Y, Mizumoto K (1998). "Cloning and characterization of three human cDNAs encoding mRNA (guanine-7-)-methyltransferase, an mRNA cap methylase". Biochem. Biophys. Res. Commun. 251 (1): 27–34. doi:10.1006/bbrc.1998.9402. PMID 9790902.
  • Saha N, Schwer B, Shuman S (1999). "Characterization of human, Schizosaccharomyces pombe, and Candida albicans mRNA cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes". J. Biol. Chem. 274 (23): 16553–62. doi:10.1074/jbc.274.23.16553. PMID 10347220.
  • Yamada-Okabe T, Mio T, Kashima Y, et al. (2000). "The Candida albicans gene for mRNA 5-cap methyltransferase: identification of additional residues essential for catalysis". Microbiology. 145 (11): 3023–33. doi:10.1099/00221287-145-11-3023. PMID 10589710.
  • Wen Y, Shatkin AJ (2001). "Cap methyltransferase selective binding and methylation of GpppG-RNA are stimulated by importin-α". Genes Dev. 14 (23): 2944–9. doi:10.1101/gad.848200. PMC 317093. PMID 11114884.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Shafer B, Chu C, Shatkin AJ (2005). "Human mRNA Cap Methyltransferase: Alternative Nuclear Localization Signal Motifs Ensure Nuclear Localization Required for Viability". Mol. Cell. Biol. 25 (7): 2644–9. doi:10.1128/MCB.25.7.2644-2649.2005. PMC 1061643. PMID 15767670.


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