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Titolo:
Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3 '-end processing machinery
Autore:
Chen, ZY; Li, YZ; Krug, RM;
Indirizzi:
Rutgers State Univ, Dept Mol Biol & Biochem, Piscataway, NJ 08855 USA Rutgers State Univ Piscataway NJ USA 08855 chem, Piscataway, NJ 08855 USA
Titolo Testata:
EMBO JOURNAL
fascicolo: 8, volume: 18, anno: 1999,
pagine: 2273 - 2283
SICI:
0261-4189(19990415)18:8<2273:IAVNPT>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
PRE-MESSENGER-RNA; NUCLEOCYTOPLASMIC TRANSPORT; NUCLEAR EXPORT; A VIRUSES; POLY(A) POLYMERASE; BINDING-PROTEIN; INFECTED-CELLS; POLYADENYLATION; CLEAVAGE; CYTOPLASM;
Keywords:
influenza virus NS1 protein; PABII; poly(A) elongation; pre-mRNA 3 '-end processing;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Krug, RM Rutgers State Univ, Dept Mol Biol & Biochem, Piscataway, NJ 08855USA Rutgers State Univ Piscataway NJ USA 08855 cataway, NJ 08855 USA
Citazione:
Z.Y. Chen et al., "Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3 '-end processing machinery", EMBO J, 18(8), 1999, pp. 2273-2283

Abstract

Influenza A virus NS1 protein (NS1A protein) via its effector domain targets the poly(A)-binding protein II (PABII) of the cellular 3'-end processingmachinery. In vitro the NS1A protein binds the PABII protein, and in vivo causes PABII protein molecules to relocalize from nuclear speckles to a uniform distribution throughout the nucleoplasm. In vitro the NS1A protein inhibits the ability of PABII to stimulate the processive synthesis of long poly(A) tails catalyzed by poly(A) polymerase (PAP), Such inhibition also occurs in vivo in influenza virus-infected cells, where the NS1A protein via its effector domain causes the nuclear accumulation of cellular pre-mRNAs which contain short (similar to 12 nucleotide) poly(A) tails. Consequently, although the NS1A protein also binds the 30 kDa subunit of the cleavage and polyadenylation specificity factor (CPSF), 3' cleavage of some cellular pre-mRNAs still occurs in virus-infected cells, followed by the PAP-catalyzed addition of short poly(A) tails. Subsequent elongation of these short poly(A) tails is blocked because the NS1A protein inhibits PABII function. Nuclear-cytoplasmic shuttling of PABII, an activity implicating this protein in the nuclear export of cellular mRNAs, is also inhibited by the NS1A protein, lit vitro assays suggest that the 30 kDa CPSF and PABII proteins bind to non-overlapping regions of the NS1A protein effector domain and indicate that these two 3' processing proteins also directly bind to each other.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 14:40:46