Heat-inducible human factor that binds to a human hsp70 promoter.
نویسندگان
چکیده
منابع مشابه
A heat-inducible nuclear factor that binds to the heat-shock element of the human haem oxygenase gene.
Haem oxygenase is a heat-shock protein in several rat tissues, as well as in certain human cells such as Hep3B hepatoma cells. In common with other heat-shock-protein genes, both the human and the rat haem oxygenase genes contain a heat-shock element (HSE) in their promoter regions. In the present study we have identified a factor in nuclear extracts of human Hep3B cells which binds specificall...
متن کاملIdentification of an inducible factor that binds to a positive regulatory element of the human beta-interferon gene.
Human beta-interferon gene expression is induced by virus or poly(I).poly(C). This induction is due at least in part to an increase in the rate of transcription and does not require protein synthesis. A 40-base-pair DNA sequence within the beta-interferon promoter, termed the interferon gene regulatory element (IRE), is an inducible enhancer in mouse fibroblasts, and both positive and negative ...
متن کاملThe human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression.
Transcriptional regulation of the human hsp70 gene in response to heat shock and other forms of physiological stress occurs through the activation of heat shock transcription factor (HSF). Exposure of cells to a heat shock temperature of 42 degrees C results in transient activation of HSF; its DNA-binding activity increases rapidly, plateaus, and attenuates, during which the intracellular level...
متن کاملHuman transcription factor IIIC binds to its cognate promoter sequences in a metal coordinated fashion.
Transcription factor IIIC from human cells (hTFIIIC) contains a 55 kDa polypeptide which specifically binds to the promoter of the VAI and 5S gene. This interaction can be abolished by depleting divalent metal cations from the free protein through chelation with EDTA. Prior association of the protein with its DNA-binding sequence renders the complex refractory to chelation by EDTA. Specific bin...
متن کاملFactor H binds to washed human platelets.
BACKGROUND Factor H regulates the alternative pathway of complement. The protein has three heparin-binding sites, is synthesized primarily in the liver and copurifies from platelets with thrombospondin-1. Factor H mutations at the C-terminus are associated with atypical hemolytic uremic syndrome, a condition in which platelets are consumed. Objectives The aim of this study was to investigate if...
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ژورنال
عنوان ژورنال: Molecular and Cellular Biology
سال: 1987
ISSN: 0270-7306,1098-5549
DOI: 10.1128/mcb.7.4.1530