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Titolo:
PROTEIN-DNA RECOGNITION COMPLEXES - CONSERVATION OF STRUCTURE AND BINDING-ENERGY IN THE TRANSITION-STATE
Autore:
JENJACOBSON L;
Indirizzi:
UNIV PITTSBURGH,DEPT BIOL SCI PITTSBURGH PA 15260
Titolo Testata:
Biopolymers
fascicolo: 2, volume: 44, anno: 1997,
pagine: 153 - 180
SICI:
0006-3525(1997)44:2<153:PRC-CO>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
REPRESSOR-OPERATOR INTERACTION; LAMBDA-CI REPRESSOR; ECORI RESTRICTION ENDONUCLEASE; B P50 HOMODIMER; YEAST TFIIA/TBP/DNA COMPLEX; AMP RECEPTOR PROTEIN; CRYSTAL-STRUCTURE; LAC REPRESSOR; LINEAR DIFFUSION; TRP REPRESSOR;
Keywords:
PROTEIN-DNA RECOGNITION; BINDING ENERGY; TRANSITION STATE; SEQUENCE-SPECIFIC BINDING; NONSPECIFIC BINDING; ADAPTATION; ENZYME CATALYSIS; THERMODYNAMICS;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
144
Recensione:
Indirizzi per estratti:
Citazione:
L. Jenjacobson, "PROTEIN-DNA RECOGNITION COMPLEXES - CONSERVATION OF STRUCTURE AND BINDING-ENERGY IN THE TRANSITION-STATE", Biopolymers, 44(2), 1997, pp. 153-180

Abstract

This paper considers how enzymes that catalyze reactions at specific DNA sites have been engineer ed to over come the problem of competitive inhibition by excess nonspecific binding sites on DNA. The formationof a specific protein-DNA recognition complex is discussed from both structural and thermodynamic perspectives, and contrasted with formation of nonspecific complexes. Evidence (from EcoRI and BamHI endonucleases) is presented that a wide variety of perturbations of the DNA substrate alter binding free energy but do not affect the free energy of activation for the chemical step; that is, many energetic factors contribute equally to the recognition complex and the transition-state complex. This implies that the specific recognition complex bears a close resemblance to the transition-state complex, such that very tight binding to the recognition site on the DNA substrate does not inhibit catalysis, but instead provides energy that is efficiently utilized along the path to the transition state. it is suggested that this view can be usefully extended to ''noncatalytic'' site-specific DNA-binding proteins like transcriptional activators and general transcription factors. (C) 1997 John Wiley & Sons, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/07/20 alle ore 09:02:39