Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators

Article Abstract:

Heat shock proteins (HSPs) act as chaperones for proteins and protect cells from many kinds of stress-induced cell damage. The inducible transcription of heat shock genes is a response to a large group of stress stimuli. The understanding of the roles and functions of heat shock factors (HSFs) has been incomplete, but it seems the diversity of the factors gives redundancy and specialization of stress signals. That would differentially control the rate of transcription of heat shock genes and give novel interactions with other regulatory factors. The link from cell stress to other genetic networks is extended. They may have an effect on the course of diseases. Regulation of heat shock transcriptional response cross talk is of interest as it goes between a family of heat shock factors, negative regulators and molecular chaperones.

United Kingdom, Physiological aspects, Genetic aspects, Observations, Stress (Physiology), Cellular signal transduction

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Molecular chaperones as HSF1-specific transcriptional repressors

Article Abstract:

Molecular chaperone Hsp70 and cochaperone Hdj1 interact in a direct way with the transactivation domain of HSF1 (heat shock factor). They also cut down heat shock gene transcription. Overexpression of either cuts transcription activity of a GAL4-HSF1 activation domain fusion protein that is transfected as well as endogenous HSF1. The activation of HSF1 DNA binding was not affected nor was inducible phosphorylation of HSF1. The main autoregulatory role of Hsp70 is thus negative regulation of HSF1 transcription activity.

Molecular genetics

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Negative regulation of the heat shock transcriptional response by HSBP1

Article Abstract:

Changes in heat shock factor 1 (HSF1) levels have significant impacts on living organism survival after chemical and thermal stress. The levels activate nuclear-localized heat shock factor binding protein 1 (HSBP1), which negatively affects DNA-binding and represses transactivation in mammalian cells. Tests on Caenorhabditis elegans protein demonstrated the interaction between HSF1 levels and HSBP1 as its negative regulator.

United States, DNA binding proteins

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