Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
PROTEIN-INDUCED FIT - THE CRP ACTIVATOR PROTEIN-CHANGES SEQUENCE-SPECIFIC DNA RECOGNITION BY THE CYTR REPRESSOR, A HIGHLY FLEXIBLE LACL MEMBER
Autore:
PEDERSEN H; VALENTINHANSEN P;
Indirizzi:
ODENSE UNIV,DEPT MOL BIOL,CAMPUSVEJ 55 DK-5230 ODENSE M DENMARK ODENSE UNIV,DEPT MOL BIOL DK-5230 ODENSE M DENMARK
Titolo Testata:
EMBO journal
fascicolo: 8, volume: 16, anno: 1997,
pagine: 2108 - 2118
SICI:
0261-4189(1997)16:8<2108:PF-TCA>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI K-12; CAMP RECEPTOR PROTEIN; BINDING-SITES; DEOP2 PROMOTER; NUCLEOTIDE-SEQUENCE; CRYSTAL-STRUCTURE; POU-DOMAIN; COMPLEX; GENE; SELECTION;
Keywords:
CAMP-CRP; CYTR; IN VITRO SELECTION; PROTEIN-DNA INTERACTIONS; PROTEIN-PROTEIN INTERACTIONS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
H. Pedersen e P. Valentinhansen, "PROTEIN-INDUCED FIT - THE CRP ACTIVATOR PROTEIN-CHANGES SEQUENCE-SPECIFIC DNA RECOGNITION BY THE CYTR REPRESSOR, A HIGHLY FLEXIBLE LACL MEMBER", EMBO journal, 16(8), 1997, pp. 2108-2118

Abstract

The CytR repressor and the cAMP receptor protein (CRP) bind cooperatively to several promoters in Escherichia coil to repress transcriptioninitiation, The synergistic binding is mediated by protein-protein interactions between the two regulators, Here, in vitro selection experiments have been used to examine the DNA-binding characteristics of CytR, by itself and when co-binding with cAMP-CRP. We show that the optimal CytR-binding site consists of two octamer repeats, in direct or inverted orientation, and separated by 2 bp. However, when co-binding with cAMP-CRP, CytR instead recognizes inverted repeats separated by 10-13 bp, or direct repeats separated by 1 bp. The configurations of the latter set of operators correlate well with the configurations of natural CytR targets, Thus, cAMP-CRP induces conformational changes in CytRso that the repressor fits the natural targets, Most strikingly, CytRcan adopt widely different conformations that are equally favored energetically for complex formation with cAMP-CRP. We propose that this structural adaptability is essential for CytR repression of promoters with diverse architectures, We discuss these novel concepts in the context of the CRP/CytR regulatory system, as well as the structural and functional implications for multiprotein-DNA complex formation in general.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 06:51:57