Properties and partial characterization of the heat-shock factor from Tetrahymena pyriformis |
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| Authors: | M do C Avides C E Sunkel P Moradas-Ferreira C Rodrigues-Pousada |
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| Institution: | Laboratório de Bioquimica, Instituto de Ciências Biomédicas Abel Salazar, Universidade do Porto, Portugal. |
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| Abstract: | A heat-shock-factor-binding activity was identified in Tetrahymena pyriformis whole-cell extracts and was further purified by sequential heparin-agarose and sequence-specific oligonucleotide affinity chromatography. Tetrahymena heat-shock factor (HSF) was able to bind to the heat-shock elements (HSE) both before and after thermal stress, although heat shock altered both the HSE-binding affinity and the protein.DNA-complex mobility on polyacrylamide gels. The mobility difference was significantly reduced by treatment of the proteins with phosphatase. The HSE-binding proteins, isolated by oligonucleotide-affinity chromatography, migrated on SDS/polyacrylamide gels as a closely spaced doublet to about 70 kDa. Polypeptides with similar molecular mass were recovered from preparative band-shift gels indicating that both are components of the protein.DNA complex. |
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