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Titolo:
SOLUTION OLIGOMERIZATION OF THE REV PROTEIN OF HIV-1 - IMPLICATIONS FOR FUNCTION
Autore:
COLE JL; GEHMAN JD; SHAFER JA; KUO LC;
Indirizzi:
MERCK RES LABS,DEPT BIOL CHEM W POINT PA 19486
Titolo Testata:
Biochemistry
fascicolo: 44, volume: 32, anno: 1993,
pagine: 11769 - 11775
SICI:
0006-2960(1993)32:44<11769:SOOTRP>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; GENE-EXPRESSION REQUIRES; RNA-BINDING; VIRION EXPRESSION; RESPONSE ELEMENT; TARGET SEQUENCE; MESSENGER-RNA; TYPE-1; REGION; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
J.L. Cole et al., "SOLUTION OLIGOMERIZATION OF THE REV PROTEIN OF HIV-1 - IMPLICATIONS FOR FUNCTION", Biochemistry, 32(44), 1993, pp. 11769-11775

Abstract

rev is an RNA-binding protein of human immunodeficiency virus-I and is required for the expression of incompletely spliced viral transcripts. Oligomerization of rev is thought to be associated with RNA bindingand rev function. Here, we have characterized the oligomerization of rev using equilibrium analytical centrifugation. rev is predominantly monomeric at low concentrations, but reversibly polymerizes to producelarge aggregates at higher concentrations. The data fit well to an unlimited isodesmic self-association model in which the association constants for the addition of a monomer to each aggregate are equal [K = 1.08 x 10(6) M-1 at 4-degrees-C]. The association constant is essentially independent of monovalent salt concentration from 0.15 to 2 M at pH6-9. Thermodynamic parameters derived from the temperature dependenceof the association constant over the limited range of 0-30-degrees-C reveal that the primary contribution to the free energy of oligomerization is a large negative enthalpy. Binding of rev to the rev-responsive element of RNA was characterized under the same conditions as the centrifugation experiments using a nitrocellulose filter assay. rev binds to the RRE at a protein concentration where rev is predominantly monomeric, suggesting that solution multimerization of rev is not required for rev function.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 08:23:45