Hsp70 structure, function, regulation and influence on yeast prions.
Heat shock proteins protect cells from various conditions of stress. Hsp70, the most ubiquitous and highly conserved Hsp, helps proteins adopt native conformation or regain function after misfolding. Various co-chaperones specify Hsp70 function and broaden its substrate range. We discuss Hsp70 structure and function, regulation by co-factors and influence on propagation of yeast prions.
Sharma
Deepak
D
Laboratory of Biochemistry and Genetics, National Institute of Diabetes, Digestive and Kidney Diseases, National institutes of Health, Bethesda, MD 20892-0851, USA.
Masison
Daniel C
DC
D005656:Fungal Proteins / Q000737:chemistry / Q000502:physiology; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000502:physiology*; D018832:Molecular Chaperones / Q000737:chemistry / Q000502:physiology; D011328:Prions / Q000502:physiology*; D011487:Protein Conformation; D017510:Protein Folding; D015003:Yeasts / Q000502:physiology*
D005656:Fungal Proteins; D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; D011328:Prions