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Titolo:
YEAST MESSENGER-RNA CAP METHYLTRANSFERASE IS A 50-KILODALTON PROTEIN ENCODED BY AN ESSENTIAL GENE
Autore:
MAO XD; SCHWER B; SHUMAN S;
Indirizzi:
SLOAN KETTERING INST,PROGRAM MOLEC BIOL NEW YORK NY 10021 SLOAN KETTERING INST,PROGRAM MOLEC BIOL NEW YORK NY 10021 UNIV MED & DENT NEW JERSEY,ROBERT WOOD JOHNSON MED SCH,DEPT BIOCHEM PISCATAWAY NJ 08854
Titolo Testata:
Molecular and cellular biology
fascicolo: 8, volume: 15, anno: 1995,
pagine: 4167 - 4174
SICI:
0270-7306(1995)15:8<4167:YMCMIA>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
RNA CAPPING ENZYME; VIRUS MESSENGER-RNA; HOST RANGE MUTANTS; VACCINIA VIRUS; SACCHAROMYCES-CEREVISIAE; SPLICING INVITRO; ESCHERICHIA-COLI; SUBUNIT; GUANYLYLTRANSFERASE; SEQUENCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
54
Recensione:
Indirizzi per estratti:
Citazione:
X.D. Mao et al., "YEAST MESSENGER-RNA CAP METHYLTRANSFERASE IS A 50-KILODALTON PROTEIN ENCODED BY AN ESSENTIAL GENE", Molecular and cellular biology, 15(8), 1995, pp. 4167-4174

Abstract

RNA (guanine-7-)methyltransferase, the enzyme responsible for methylating the 5' cap structure of eukaryotic mRNA, was isolated from extracts of Saccharomyces cerevisiae. The yeast enzyme catalyzed methyl group transfer from S-adenosyl-L-methionine to the guanosine base of capped, unmethylated poly(A). Cap methylation was stimulated by low concentrations of salt and was inhibited by S-adenosyl-L-homocysteine, a presumptive product of the reaction, but not by S-adenosyl-D-homocysteine. The methyltransferase sedimented in a glycerol gradient as a single discrete component of 3.2S. A likely candidate for the gene encoding yeast cap methyltransferase was singled out on phylogenetic grounds. TheABD1 gene, located on yeast chromosome II, encodes a 436-amino-acid (50-kDa) polypeptide that displays regional similarity to the catalyticdomain of the vaccinia virus cap methyltransferase. That the ABD1 gene product is indeed RNA (guanine-7-)methyltransferase was established by expressing the ABD1 protein in bacteria, purifying the protein to homogeneity, and characterizing the cap methyltransferase activity intrinsic to recombinant ABD1. The physical and biochemical properties of recombinant ABD1 methyltransferase were indistinguishable from those of the cap methyltransferase isolated and partially purified from wholecell yeast extracts. Our finding that the ABD1 gene is required for yeast growth provides the first genetic evidence that a cap methyltransferase (and, by inference, the cap methyl group) plays an essential role in cellular function in vivo.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 01:40:28