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Progress in J-domain Protein
Guo-Liang Li , Bing Li1, Wei Zhou1, Ren-Gang Zhou*
Institute of Genetics and Physiology, Hebei Academy of Agricultural Sciences, Shijiazhuang 050051, China; 1College of Life Sciences, Hebei Normal University, Shijiazhuang 050016, China
Abstract: The characteristic feature of J-domain protein is the presence of the J-domain， a conserved approximately 75 amino acid sequence that forms multiple α-helices. The invariant tripeptide， HPD， is both characteristic and absolutely essential for the biological function of J-domain protein. The G/F-rich sequence proximal to the J-domain functions as a flexible linker region. Four repeats of CxxCxGxG together comprise the zinc-finger-like domain. J-domain proteins can function as co-chaperones in conjunction with HSP70 or in a multi-protein chaperone machine. J-domain protein and HSP70 cooperate in many cellular processes， including protein folding， translocation and signal transduction. The Arabidopsis thaliana genome includes a large and diverse family of J-domain proteins. The 94 A. thaliana J-domain proteins， which have been divided into 51 families， are located in nucleus; cytoplasm; mitochondria; plastid; membrane and peroxisome respectively in the cell. The A. thaliana J-domain proteins are involved in response to many environmental stresses and physiological processes.
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