Multimerization of Hsp42p, a Novel Heat Shock Protein of Saccharomyces cerevisiae, Is Dependent on a Conserved Carboxyl-terminal Sequence

• DOI: 10.1074/jbc.271.5.2717
• Publication Date: 2002-07-26T15:15:23Z
• Authors: David Wotton; Katie Freeman; David Shore
• Keywords: Homology

Rap1p is a transcriptional regulator of Saccharomyces cerevisiae, which plays roles in both activation and silencing. To identify proteins involved Rap1p-dependent regulation transcription, we used the two-hybrid system to screen for Rap1p-interacting proteins. Two clones isolated from this encode truncated protein with homology small heat shock (HSPs). Here present an analysis novel S. cerevisiae HSP, name Hsp42p. Expression HSP42 regulated by range stress conditions similar HSP26, Hsp42p shares most homology. However, expression more sensitive increased salt concentration starvation and, contrast HSP26 expressed unstressed cells. interacts itself assay. This interaction dependent on hydrophobic region conserved among HSPs. Using bacterially fusion proteins, demonstrate that direct interaction. Fractionation yeast extracts size demonstrates all these complexes molecular mass greater than 200 kDa, suggesting exists high complexes.