PMID:15170475

Citation	Walsh, P, Bursać, D, Law, YC, Cyr, D and Lithgow, T (2004) The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep. 5:567-71
Abstract	DnaJ 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.
Links	PubMed PMC1299080 Online version:10.1038/sj.embor.7400172
Keywords	Amino Acid Sequence; Genome, Fungal; Heat-Shock Proteins/classification; Heat-Shock Proteins/physiology; Molecular Chaperones/classification; Molecular Chaperones/physiology; Molecular Sequence Data; Protein Structure, Tertiary; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins/classification; Saccharomyces cerevisiae Proteins/physiology; Sequence Alignment
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