Insights in small Heat Shock Protein/client interaction by combined protection analysis of two different client proteins.
sHSPs interact with clients under denaturing conditions. CPH1Δ2, 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.
Institute for Plant Physiology, Justus-Liebig University Giessen, Germany. Benjamin.Eisenhardt@bio.uni-giessen.de
Benjamin D
BD
Eisenhardt
Christoph
C
Forreiter
D017360:Arabidopsis / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D000458:Cyanobacteria / Q000378:metabolism; D050888:Heat-Shock Proteins, Small / Q000737:chemistry* / Q000378:metabolism*; D008291:Malate Dehydrogenase / Q000737:chemistry / Q000378:metabolism; D010834:Phytochrome / Q000737:chemistry / Q000378:metabolism*
D029681:Arabidopsis Proteins; D001426:Bacterial Proteins; D050888:Heat-Shock Proteins, Small; D010834:Phytochrome; D008291:Malate Dehydrogenase