Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Binding of phage-displayed HIV-1 Tat to TAR RNA in the presence of cyclin T1
Autore:
Jonas, G; Hoffmann, S; Willbold, D;
Indirizzi:
Inst Mol Biotechnol, Jena, Germany Inst Mol Biotechnol Jena GermanyInst Mol Biotechnol, Jena, Germany Univ Bayreuth, Lehrstuhl Biopolymere, D-95440 Bayreuth, Germany Univ Bayreuth Bayreuth Germany D-95440 lymere, D-95440 Bayreuth, Germany
Titolo Testata:
JOURNAL OF BIOMEDICAL SCIENCE
fascicolo: 5, volume: 8, anno: 2001,
pagine: 430 - 436
SICI:
1021-7770(200109)8:5<430:BOPHTT>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; TRANS-ACTIVATOR GENE; HIGH-AFFINITY; PROTEIN; COMPLEX; TRANSACTIVATION; PEPTIDE; TYPE-1; REPLICATION; RECOGNITION;
Keywords:
HIV-1; transactivator; cyclin T1; phage display; protein-RNA interactions;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Willbold, D Inst Mol Biotechnol Strukturelle & Evolut Biochem, Beutenbergstr 11, D-07745 Jena, Germany Inst Mol Biotechnol Strukturelle & Evolut Biochem Beutenbergstr 11 Jena Germany D-07745
Citazione:
G. Jonas et al., "Binding of phage-displayed HIV-1 Tat to TAR RNA in the presence of cyclin T1", J BIOMED SC, 8(5), 2001, pp. 430-436

Abstract

The transactivator protein (Tat) of the human immunodeficiency virus (HIV)is a key regulatory protein in the viral replication cycle. Together with cellular cyclin T1 and an RNA element (transactivation response; TAR) located at the 5' end of all viral transcripts, it forms a ternary complex that ultimately enhances the expression of all viral genes. In this ternary complex, cyclin T1 interacts directly with Tat and TAR. The presence of cyclin T1 is essential for high TAR RNA affinity and specificity of Tat. To study protein-protein and protein-RNA interaction, we developed a phage display system that displays functional Tat on the surface of bacteriophage M13. Theaddition of recombinant cyclin T1 to the selections yielded a phage display system that mirrors all binding properties of the cyclin T1-Tat-TAR complex known from cell assays and biochemical studies. Phage-displayed Tat protein as well as the cyclin T1 are fully functional. The relative binding capabilities of wild-type- and mutant Tat-displaying phages show that the presence of cyclin T1 significantly reduces the importance of basic residues inthe basic sequence region of Tat for its binding to TAR. Copyright (C) 2001 National Science Council, ROC and S. Karger AG, Basel.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/01/20 alle ore 08:17:42