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Titolo:
Enolase, a cellular glycolytic enzyme, is required for efficient transcription of Sendai virus genome
Autore:
Ogino, T; Yamadera, T; Nonaka, T; Imajoh-Ohmi, S; Mizumoto, K;
Indirizzi:
Kitasato Univ, Sch Pharmaceut Sci, Dept Biochem, Minato Ku, Tokyo 1088641,Japan Kitasato Univ Tokyo Japan 1088641 iochem, Minato Ku, Tokyo 1088641,Japan Kitasato Inst, Res Ctr Biol, Minato Ku, Tokyo 1088642, Japan Kitasato Inst Tokyo Japan 1088642 Biol, Minato Ku, Tokyo 1088642, Japan Univ Tokyo, Inst Med Sci, Dept Basic Med Sci, Div Mol Cell Signaling,Minato Ku, Tokyo 1088639, Japan Univ Tokyo Tokyo Japan 1088639 Signaling,Minato Ku, Tokyo 1088639, Japan
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 2, volume: 285, anno: 2001,
pagine: 447 - 455
SICI:
0006-291X(20010713)285:2<447:EACGEI>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
RESPIRATORY SYNCYTIAL VIRUS; MUSCLE-SPECIFIC ENOLASE; MESSENGER-RNA SYNTHESIS; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; ALPHA-ENOLASE; IN-VITRO; HUMAN GENE; PHOSPHOGLYCERATE KINASE; NUCLEOTIDE-SEQUENCE; INVITRO SYSTEM;
Keywords:
paramyxovirus; Sendai virus; transcription; replication; host factor; cytoskeletal protein; tubulin; glycolytic enzyme; phosphoglycerate kinase (PGK); enolase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Mizumoto, K Kitasato Univ, Sch Pharmaceut Sci, Dept Biochem, Minato Ku, 5-9-1 Shirokane, Tokyo 1088641, Japan Kitasato Univ 5-9-1 Shirokane Tokyo Japan 1088641 8641, Japan
Citazione:
T. Ogino et al., "Enolase, a cellular glycolytic enzyme, is required for efficient transcription of Sendai virus genome", BIOC BIOP R, 285(2), 2001, pp. 447-455

Abstract

Cellular proteins (host factors) may play key roles in transcription of Sendai virus (SeV) genome. We have previously shown that the host factor activity, which stimulates in vitro mRNA synthesis of SeV, from bovine brain comprises at least three complementary factors, and two of them were identified as tubulin and phosphoglycerate kinase (PGK), Here the third host factoractivity was further resolved into two complementary factors, and one of them was purified to an almost single polypeptide chain with an apparent 2M,of 52,000 (p52) and was identified as a glycolytic enzyme, enolase, Recombinant human alpha -enolase, as did p52, acted synergistically with other three host factors to stimulate SeV mRNA synthesis. West-Western blot analysis demonstrated that tubulin specifically binds enolase as well as PGK, suggesting that these two glycolytic enzymes regulate SeV transcription throughtheir interactions with tubulin. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 11:46:49