The Yeast Hsp110 Sse1 Functionally Interacts with the Hsp70 Chaperones Ssa and Ssb

• Published in: The Journal of biological chemistry Vol. 280; no. 50; pp. 41262 - 41269
• Main Authors: Shaner, Lance, Wegele, Harald, Buchner, Johannes, Morano, Kevin A.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 16.12.2005; American Society for Biochemistry and Molecular Biology
• Subjects: Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - metabolism; Alleles; Cytosol - metabolism; Dimerization; DNA Mutational Analysis; DNA-Binding Proteins - metabolism; Electrophoresis, Polyacrylamide Gel; Endoplasmic Reticulum - metabolism; Fungal Proteins - metabolism; HSP110 Heat-Shock Proteins - metabolism; HSP110 Heat-Shock Proteins - physiology; HSP40 Heat-Shock Proteins - metabolism; HSP70 Heat-Shock Proteins - metabolism; HSP90 Heat-Shock Proteins - metabolism; Immunoblotting; Immunoprecipitation; Molecular Chaperones - metabolism; Mutation; Peptides - chemistry; Plasmids - metabolism; Point Mutation; Protein Binding; Protein Biosynthesis; Protein Precursors - chemistry; Protein Processing, Post-Translational; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - metabolism; Saccharomyces cerevisiae Proteins - physiology; Signal Transduction; Transcription, Genetic

There is growing evidence that members of the extended Hsp70 family of molecular chaperones, including the Hsp110 and Grp170 subgroups, collaborate in vivo to carry out essential cellular processes. However, relatively little is known regarding the interactions and cellular functions of Sse1, the ye...