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Titolo:
PROBING THE DETAILS OF THE HIV-1 REV-REV-RESPONSIVE ELEMENT INTERACTION - EFFECTS OF MODIFIED NUCLEOTIDES ON PROTEIN AFFINITY AND CONFORMATIONAL-CHANGES DURING COMPLEX-FORMATION
Autore:
RENWICK SB; CRITCHLEY AD; ADAMS CJ; KELLY SM; PRICE NC; STOCKLEY PG;
Indirizzi:
UNIV LEEDS,DEPT GENET LEEDS LS2 9JT W YORKSHIRE ENGLAND UNIV LEEDS,DEPT GENET LEEDS LS2 9JT W YORKSHIRE ENGLAND UNIV STIRLING,DEPT BIOL & MOLEC SCI STIRLING FK9 4LA SCOTLAND
Titolo Testata:
Biochemical journal
, volume: 308, anno: 1995,
parte:, 2
pagine: 447 - 453
SICI:
0264-6021(1995)308:<447:PTDOTH>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; GENE-EXPRESSION REQUIRES; RNA-BINDING SITE; VIRION EXPRESSION; TRANS-ACTIVATOR; TARGET SEQUENCE; MESSENGER-RNA; STEM-LOOP; RECOGNITION; REGION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
S.B. Renwick et al., "PROBING THE DETAILS OF THE HIV-1 REV-REV-RESPONSIVE ELEMENT INTERACTION - EFFECTS OF MODIFIED NUCLEOTIDES ON PROTEIN AFFINITY AND CONFORMATIONAL-CHANGES DURING COMPLEX-FORMATION", Biochemical journal, 308, 1995, pp. 447-453

Abstract

The solution structure of the human immunodeficiency virus type 1 (HIV-1) Rev-responsive element (RRE) has been investigated by enzymic andchemical structural probing of a 71 nt RRE transcript, The minimum sequence information required to maintain recognition by the Rev proteinhas previously been mapped to a 29 nt stem-loop structure, known as minSLIIB. The key recognition target is a single-stranded RNA bubble atthe base of the RNA stem. The fine details of RNA recognition have been probed using chemically synthesized minSLIIBs containing variant base or sugar residues at sites within the bubble. These have been analysed by gel retardation assays and their relative affinities for Rev protein determined, Complex formation between the wild-type minSLIIB RREand Rev protein was also monitored using CD spectroscopy, which suggests a change in RNA conformation upon Rev binding. The spectral changeis consistent with localized melting of RNA, leading to a decrease inthe level of base stacking and/or a change in base tilting, during formation of the complex. Deoxynucleotide substitutions on just one side, the 5' side, of the bubble inhibit the conformational change detected by CD. The data are consistent with a dynamic interaction between Rev and its target site. The contact points between Rev and the RRE wereprobed directly using photo-cross-linking with either ribo-5-bromouridine- or ribo-4-thiouridine-substituted minSLIIBs. The data are consistent with protein-RNA contacts at the bottom of the bubble.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 09:22:24