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Nucleotide Binding by Lhs1p Is Essential for Its Nucleotide Exchange Activity and for Function in Vivo

Protein translocation and folding in the endoplasmic reticulum of Saccharomyces cerevisiae involves two distinct Hsp70 chaperones, Lhs1p and Kar2p. Both proteins have the characteristic domain structure of the Hsp70 family consisting of a conserved N-terminal nucleotide binding domain and a C-termin...

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Detalles Bibliográficos
Autores principales:	de Keyzer, Jeanine, Steel, Gregor J., Hale, Sarah J., Humphries, Daniel, Stirling, Colin J.
Formato:	Texto
Lenguaje:	English
Publicado:	American Society for Biochemistry and Molecular Biology 2009
Materias:	Protein Structure and Folding
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2797226/ https://www.ncbi.nlm.nih.gov/pubmed/19759005 http://dx.doi.org/10.1074/jbc.M109.055160

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