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Titolo:
Recruitment of HU by piggyback: a special role of GalR in repressosome assembly
Autore:
Kar, S; Adhya, S;
Indirizzi:
NCI, Dept Mol Biol, NIH, Bethesda, MD 20892 USA NCI Bethesda MD USA 20892NCI, Dept Mol Biol, NIH, Bethesda, MD 20892 USA
Titolo Testata:
GENES & DEVELOPMENT
fascicolo: 17, volume: 15, anno: 2001,
pagine: 2273 - 2281
SICI:
0890-9369(20010901)15:17<2273:ROHBPA>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
HISTONE-LIKE PROTEINS; ESCHERICHIA-COLI; DNA-BINDING; HOMOLOGOUS RECOMBINATION; TRANSCRIPTION FACTORS; COMPLEX; PROMOTE; HMG1; INTERACTS; INVITRO;
Keywords:
transcription repression; DNA looping; protein-protein interaction; HU mutants;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Adhya, S NCI, Dept Mol Biol, NIH, Bethesda, MD 20892 USA NCI Bethesda MD USA 20892 Mol Biol, NIH, Bethesda, MD 20892 USA
Citazione:
S. Kar e S. Adhya, "Recruitment of HU by piggyback: a special role of GalR in repressosome assembly", GENE DEV, 15(17), 2001, pp. 2273-2281

Abstract

In Gal repressosome assembly, a DNA loop is formed by the interaction of two GalR, bound to two distal operators, and the binding of the histone-likeprotein, HU, to an architecturally critical position on DNA to facilitate the GalR-GalR interaction. We show that GalR piggybacks HU to the critical position on the DNA through a specific GalR-HU interaction. This is the first example of HU making a specific contact with another protein. The GaIR-HU contact that results in cooperative binding of the two proteins to DNA may be transient and absent in the final repressosome structure. A sequence-independent DNA-binding protein being recruited to an architectural site on DNA through a specific association with a regulatory protein may be a common mode for assembly of complex nucleoprotein structures.

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Documento generato il 11/07/20 alle ore 17:09:06