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Insights in small Heat Shock Protein/client interaction by combined protection analysis of two different client proteins


, : Insights in small Heat Shock Protein/client interaction by combined protection analysis of two different client proteins. Febs Letters 586(13): 1772-1777

SHSPs interact with clients under denaturing conditions. CPH1?2, a truncated version of cyanobacterial phytochrome CPH1, was introduced as a new reporter (client). Comparative analyses of At17.8 and At17.6B as cytosolic class I sHSP representatives demonstrated the advantages of a chromophore-bearing photoreversible protein as new client for analyzing sHSP holdase function in addition to malate dehydrogenase (MDH). The tested sHSPs protected both clients in similar ways but with different efficiencies. Bis-ANS binding studies with sHSPs suggested that the bis-ANS binding is dependent on interactions between different sHSPs and MDH under denaturing temperatures. Structured summary of protein interactions CPH1?2 and CPH1?2 bind by molecular sieving (View interaction)CPH1?2 and HSP17.8 bind by molecular sieving (View interaction)CPH1?2 and HSP17.6 bind by molecular sieving (View interaction)MDH and HSP17.8 bind by molecular sieving (View interaction)MDH and HSP17.6B bind by molecular sieving (View interaction).

US$19.90

PMID: 22641032

DOI: 10.1016/j.febslet.2012.05.022


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