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The effect of polypeptide binding on the stability of the substrate binding domain of the molecular chaperone DnaK has been studied by thermodynamic analysis. The calorimetric scan of the fragment of the substrate binding domain DnaK384–638, consisting of a β-domain and an α-helical lid, showed two transitions centered at 56.2 and 76.0 °C. On the other hand, the thermal unfolding of the shorter fragment...
The heat shock protein (Hsp) HtpG is a member of the Hsp90 protein family. We cloned a single-copy gene encoding a homologue of HtpG from the unicellular cyanobacterium Synechococcus sp. PCC 7942. Sequence alignment with HtpGs from other prokaryotes revealed unique features in the cyanobacterial HtpG primary sequence. A monocistronic mRNA of the htpG gene increased transiently in response to heat...
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