Article
The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.
The Journal of biological chemistry - 21 May 2004
Shaner Lance, Trott Amy, Goeckeler Jennifer L, Brodsky Jeffrey L, Morano Kevin A
Abstract excerpt
The Sse1/Hsp110 molecular chaperones are a poorly understood subgroup of the Hsp70 chaperone family. Hsp70 can refold denatured polypeptides via a C-terminal peptide binding domain (PBD), which is regulated by nucleotide cycling in an N-terminal ATPase domain. However, unlike Hsp70, both Sse1 and mammalian Hsp110 bind unfolded peptide substrates but cannot refold them. To test the in vivo requirement for...
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