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rdf:type |
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lifeskim:mentions |
umls-concept:C0015576,
umls-concept:C0033684,
umls-concept:C0040715,
umls-concept:C0599718,
umls-concept:C0599813,
umls-concept:C0599893,
umls-concept:C1522702,
umls-concept:C1706853,
umls-concept:C1707798,
umls-concept:C1709059,
umls-concept:C1879748,
umls-concept:C1880352
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pubmed:issue |
6
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pubmed:dateCreated |
2004-6-1
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-10441154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-10531024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-10542335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-11231140,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-11279042,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-11378903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-11395418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-11884590,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-11923285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-12454054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-12493774,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-12732306,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-12741832,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-12847107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-14562095,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-14656429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-14657253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-14973134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-7972061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-8764402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-9199165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-9242927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-9476895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-9585179,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-9600925,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-9644977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-9679141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-9774392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-9817751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15170475-9922173
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1469-221X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
567-71
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15170475-Amino Acid Sequence,
pubmed-meshheading:15170475-Genome, Fungal,
pubmed-meshheading:15170475-Heat-Shock Proteins,
pubmed-meshheading:15170475-Molecular Chaperones,
pubmed-meshheading:15170475-Molecular Sequence Data,
pubmed-meshheading:15170475-Protein Structure, Tertiary,
pubmed-meshheading:15170475-Saccharomyces cerevisiae,
pubmed-meshheading:15170475-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:15170475-Sequence Alignment
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pubmed:year |
2004
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pubmed:articleTitle |
The J-protein family: modulating protein assembly, disassembly and translocation.
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pubmed:affiliation |
Russell Grimwade School of Biochemistry and Molecular Biology, University of Melbourne, Melbourne 3010, Australia.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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