| Autor: |
Walsh, Peter, Bursac, Dejan, Yin Chern Law, Cyr, Douglas, Lithgow, Trevor |
| Předmět: |
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| Zdroj: |
EMBO Reports; Jun2004, Vol. 5 Issue 6, p567-571, 5p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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