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Titolo:
PREFERENTIAL INTERACTIONS OF THE ESCHERICHIA-COLI LEXA REPRESSOR WITHANIONS AND PROTONS ARE COUPLED TO BINDING THE RECA OPERATOR
Autore:
RELAN NK; JENUWINE ES; GUMBS OH; SHANER SL;
Indirizzi:
WAYNE STATE UNIV,DEPT CHEM DETROIT MI 48202 WAYNE STATE UNIV,DEPT CHEM DETROIT MI 48202
Titolo Testata:
Biochemistry
fascicolo: 5, volume: 36, anno: 1997,
pagine: 1077 - 1084
SICI:
0006-2960(1997)36:5<1077:PIOTEL>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-TERMINAL DOMAIN; MOBILITY-SHIFT ASSAY; NUCLEIC-ACIDS; GEL-ELECTROPHORESIS; NUCLEOTIDE-SEQUENCE; REGULATORY SYSTEM; LAC REPRESSOR; DNA; PROTEIN; GENE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
51
Recensione:
Indirizzi per estratti:
Citazione:
N.K. Relan et al., "PREFERENTIAL INTERACTIONS OF THE ESCHERICHIA-COLI LEXA REPRESSOR WITHANIONS AND PROTONS ARE COUPLED TO BINDING THE RECA OPERATOR", Biochemistry, 36(5), 1997, pp. 1077-1084

Abstract

The binding of Escherichia coli LexA repressor to the recA operator was examined as a function of the concentration of NaCl, KCl, NaF, and MgCl2 at pH 7.5, 21 degrees C. The effects of pH at 100 mM NaCl were also examined. Changes both in the qualitative appearance of the binding isotherms and in the magnitude of the apparent binding affinity withchanges in solution conditions suggest that binding of anions and protons by LexA repressor is linked to oligomerization and/or operator binding. Binding of LexA repressor to the recA operator in the presence of NaCl ranging from 25 to 400 mM at picomolar DNA concentration showed a broad, apparently noncooperative, binding isotherm. Binding of LexA repressor in NaF at the same [DNA] yielded binding isotherms with a narrow transition, reflecting an apparently cooperative binding process. Also, the apparent binding affinity was weaker in NaF than in NaCl Furthermore, the binding affinity and also the apparent binding mode, cooperative vs noncooperative, were pH dependent. The binding affinityof LexA repressor for operator was greatest near neutral pH. The apparent binding mode was noncooperative at pH 7-9 but was cooperative at pH 6 or 9.3. These observations suggest that the specific cation and anion composition and concentrations must be considered in understanding the details of regulation of the SOS system.

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Documento generato il 03/04/20 alle ore 20:36:18