UV cross-linking of distinct proteins to the PRDII domain of the interferon-beta promoter

Journal Article · Fri Mar 30 04:00:00 EST 1990 · Biochemical and Biophysical Research Communications; (USA)

DOI:https://doi.org/10.1016/0006-291X(90)90634-Y· OSTI ID:6833805

Xanthoudakis, S; Hiscott, J ^[1]

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1. Sir Mortimer B. Davis Jewish General Hospital, Montreal, Quebec (Canada)

The human interferon-beta gene (IFN-beta) is transcriptionally activated in a variety of cell types, mediated in part by a decameric element, designated the PRDII domain (-55 to -64) which is the target for the transcription factor NF-kappa B. In the present study, we have examined factor binding to the PRDII domain in three cell lines (HeLa, U937, Jurkat) following treatment with known inducers of IFN-beta transcription and NF-kappa B binding activity. UV cross-linking analysis has revealed that in all 3 cell types two inducible proteins of 58 kD and 69 kD and one constitutive protein of 48 kD bind to the PRDII domain. These experiments suggest that multiple proteins may interact with this element to regulate IFN-beta gene transcription.

• OSTI ID: 6833805
• Journal Information: Biochemical and Biophysical Research Communications; (USA), Journal Name: Biochemical and Biophysical Research Communications; (USA) Vol. 167:3; ISSN BBRCA; ISSN 0006-291X
• Country of Publication: United States
• Language: English

Related Subjects

560120* -- Radiation Effects on Biochemicals
Cells
& Tissue Culture
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
ANIMALS
BIOLOGICAL EFFECTS
CARCINOGENS
CHEMICAL RADIATION EFFECTS
CHEMICAL REACTIONS
CHEMISTRY
CROSS-LINKING
ELECTROMAGNETIC RADIATION
ESTERS
GENE REGULATION
GENES
GROWTH FACTORS
HELA CELLS
INTERFERON
LYMPHOKINES
MAMMALS
MAN
MITOGENS
NUCLEIC ACIDS
OLIGONUCLEOTIDES
ORGANIC COMPOUNDS
PHORBOL ESTERS
POLYMERIZATION
PRIMATES
PROTEINS
RADIATION CHEMISTRY
RADIATION EFFECTS
RADIATIONS
REAGENTS
TRANSCRIPTION
ULTRAVIOLET RADIATION
VERTEBRATES