On the path to the heat shock response: destabilization and formation of partially folded protein intermediates, a consequence of protein thiol modification.
This review discusses the initial events that occur during oxidative stress that induce the synthesis of heat shock proteins. The focus is on non-native oxidation or modification of protein thiols and the destablization that can result. Proteins that contain non-native modified thiols can become destablized such that they unfold into molten globule-like intermediates at or below 37 degrees C, relieving Hsf-1 negative regulation, and inducing Hsp transcription.
Freeman
M L
ML
Department of Radiation Oncology, Vanderbilt Cancer Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USA. Michael.Freeman@mcmail.vanderbilt.edu
Borrelli
M J
MJ
Meredith
M J
MJ
Lepock
J R
JR
D000818:Animals; D006360:Heat-Shock Proteins / Q000096:biosynthesis* / Q000502:physiology; D006358:Hot Temperature; D006801:Humans; D008322:Mammals; D018832:Molecular Chaperones / Q000502:physiology; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D017510:Protein Folding; D011506:Proteins / Q000378:metabolism; D013438:Sulfhydryl Compounds
D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D011506:Proteins; D013438:Sulfhydryl Compounds