In the cell, the molecular chaperone Hsp90 governs the folding of unstable proteins, such as signal transduction kinases and transcription factors. To fulfill this task, it interacts with several cochaperones in a folding cycle. In baker’s yeast, Cns1 is one of these cochaperones. This work describes the interaction of Cns1 with Ssa1 and Hsp90. Cns1 stimulates the ATPase activity of Ssa1. The N-terminal domain of Cns1 is crucial for this effect and for the viability in yeast. In a second project, the charged N-M domain linker of Hsp90 is characterized. This linker can only be found in eucaryotic Hsp90. Its deletion is lethal and is accompanied with a drastically reduced chaperone activity and cochaperone-mediated regulability.
«
In the cell, the molecular chaperone Hsp90 governs the folding of unstable proteins, such as signal transduction kinases and transcription factors. To fulfill this task, it interacts with several cochaperones in a folding cycle. In baker’s yeast, Cns1 is one of these cochaperones. This work describes the interaction of Cns1 with Ssa1 and Hsp90. Cns1 stimulates the ATPase activity of Ssa1. The N-terminal domain of Cns1 is crucial for this effect and for the viability in yeast. In a second project...
»