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 / EGO
Search PMC articles PubMed articles NCBI proteins

RNA (guanine-7-) methyltransferase
Rendering based on PDB 3BGV​.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3BGV​, 3EPP​
Identifiers
Symbols	RNMT ; CMT1; CMT1c; MET; Met; RG7MT1; cm1p; hCMT1; hMet
External IDs	OMIM: 603514 MGI: 1915147 HomoloGene: 2816 GeneCards: RNMT Gene
EC number	2.1.1.56
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
Entrez	8731	67897
Ensembl	ENSG00000101654	ENSMUSG00000009535
UniProt	O43148	Q9D0L8
RefSeq (mRNA)	NM_001308263	NM_001170953
RefSeq (protein)	NP_001295192	NP_001164424
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.

See also

• 7-Methylguanosine

References

1. 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.
2. 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.
3. "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): 2525–9. 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.