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The J-protein family: modulating protein assembly, disassembly and translocation Walsh P; Bursac D; Law YC; Cyr D; Lithgow TEMBO Rep 2004[Jun]; 5 (6): 567-71DnaJ is a molecular chaperone and the prototypical member of the J-protein family. J proteins are defined by the presence of a J domain that can regulate the activity of 70-kDa heat-shock proteins. Sequence analysis on the genome of Saccharomyces cerevisiae has revealed 22 proteins that establish four distinguishing structural features of the J domain: predicted helicity in segments I-IV, precisely placed interhelical contact residues, a lysine-rich surface on helix II and placement of the diagnostic sequence HPD between the predicted helices II and III. We suggest that this definition of the J-protein family could be used for other genome-wide studies. In addition, three J-like proteins were identified in yeast that contain regions closely resembling a J domain, but in which the HPD motif is non-conservatively replaced. We suggest that J-like proteins might function to regulate the activity of bona fide J proteins during protein translocation, assembly and disassembly.|Amino Acid Sequence[MESH]|Genome, Fungal[MESH]|Heat-Shock Proteins/classification/*physiology[MESH]|Molecular Chaperones/classification/*physiology[MESH]|Molecular Sequence Data[MESH]|Protein Structure, Tertiary[MESH]|Saccharomyces cerevisiae Proteins/classification/*physiology[MESH]|Saccharomyces cerevisiae/genetics/metabolism[MESH]|Sequence Alignment[MESH] |
