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Titolo:
Sequence-specific interaction between HIV-1 matrix protein and viral genomic RNA revealed by in vitro genetic selection
Autore:
Purohit, P; Dupont, S; Stevenson, M; Green, MR;
Indirizzi:
Univ Massachusetts, Med Ctr, Howard Hughes Med Inst, Program Gene Funct & Express, Worcester, MA 01605 USA Univ Massachusetts Worcester MA USA 01605xpress, Worcester, MA 01605 USA Univ Massachusetts, Med Ctr, Program Mol Med, Worcester, MA 01605 USA UnivMassachusetts Worcester MA USA 01605 ol Med, Worcester, MA 01605 USA
Titolo Testata:
RNA-A PUBLICATION OF THE RNA SOCIETY
fascicolo: 4, volume: 7, anno: 2001,
pagine: 576 - 584
SICI:
1355-8382(200104)7:4<576:SIBHMP>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; HIGH-AFFINITY BINDING; NUCLEAR-LOCALIZATION SIGNAL; TYPE-1 GAG POLYPROTEIN; NUCLEOCAPSID PROTEIN; REVERSE-TRANSCRIPTASE; MUTATIONAL ANALYSIS; VPR; INFECTION; COMPLEXES;
Keywords:
HIV; in vitro selection; matrix protein; RNA-protein interaction;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Green, MR Univ Massachusetts, Med Ctr, Howard Hughes Med Inst, Program Gene Funct & Express, 373 Plantat St,Suite 309, Worcester, MA 01605 USA Univ Massachusetts 373 Plantat St,Suite 309 Worcester MA USA 01605
Citazione:
P. Purohit et al., "Sequence-specific interaction between HIV-1 matrix protein and viral genomic RNA revealed by in vitro genetic selection", RNA, 7(4), 2001, pp. 576-584

Abstract

The human immunodeficiency virus type-1 matrix protein (HIV-1 MA) is a multifunctional structural protein synthesized as part of the Pr55 gag polyprotein, We have used in vitro genetic selection to identify an RNA consensus sequence that specifically interacts with MA (K-d = 5 x 10(-7) M), This 13-nt MA binding consensus sequence bears a high degree of homology (77%) to aregion (nt 1433-1446) within the POL open reading frame of the HIV-1 genome (consensus sequence from 38 HIV-1 strains). Chemical interference experiments identified the nucleotides within the MA binding consensus sequence involved in direct contact with MA. We further demonstrate that this RNA-protein interaction is mediated through a stretch of basic amino acids within MA. Mutations that disrupt the interaction between MA and its RNA binding site within the HIV-1 genome resulted in a measurable decrease in viral replication.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/01/20 alle ore 12:16:18