mRNA (guanine-N7-)-methyltransferase

Gene ontology
Molecular function	• RNA binding • mRNA (guanine-N7-)-methyltransferase activity • protein binding
Cellular component	• nucleus • nucleoplasm • nucleolus • mRNA cap binding complex • receptor complex
Biological process	• transcription from RNA polymerase II promoter • 7-methylguanosine mRNA capping • gene expression • viral process • RNA (guanine-N7)-methylation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 18:
13.73 – 13.76 Mb

Chr 18:
68.3 – 68.32 Mb

PubMed search

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

\rightleftharpoons

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.^[1]^[2]^[3]

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.

References

↑ 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.
↑ 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.
↑ "Entrez Gene: RNMT RNA (guanine-7-) methyltransferase".

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): 2525–9. 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): 977–82. 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): 9330–5. 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): 9322–9. 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 (Reading, Engl.) 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.

Transferase: one carbon transferases (EC 2.1)

2.1.1: Methyl-

N-	Histamine N-methyltransferase Phenylethanolamine N-methyltransferase Amine N-methyltransferase Phosphatidylethanolamine N-methyltransferase

O-	5-hydroxyindole-O-methyltransferase/Acetylserotonin O-methyltransferase Catechol-O-methyl transferase

Homocysteine	Betaine-homocysteine methyltransferase Homocysteine methyltransferase Methionine synthase

Other	Phosphatidyl ethanolamine methyltransferase DNMT3B Histone methyltransferase Thymidylate synthase DNA methyltransferase Thiopurine methyltransferase

2.1.2: Hydroxymethyl-,
Formyl- and Related

Hydroxymethyltransferase	Serine hydroxymethyltransferase 3-methyl-2-oxobutanoate hydroxymethyltransferase

Formyltransferase	Phosphoribosylglycinamide formyltransferase Inosine monophosphate synthase

Other	Glutamate formimidoyltransferase Aminomethyltransferase

2.1.3: Carboxy-
and Carbamoyl

Carboxy	methylmalonyl-CoA carboxytransferase

Carbamoyl	Aspartate carbamoyltransferase Ornithine carbamoyltransferase Oxamate carbamoyltransferase Putrescine carbamoyltransferase 3-hydroxymethylcephem carbamoyltransferase Lysine carbamoyltransferase N-acetylornithine carbamoyltransferase

2.1.4: Amidine

Arginine:glycine amidinotransferase

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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mRNA (guanine-N7-)-methyltransferase

Nomenclature

See also

References

Further reading