Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1996-8-15
pubmed:abstractText
Prions mediate the pathogenesis of certain neurodegenerative diseases, including bovine spongiform encephalopathy in cattle and Creutzfeldt-Jakob disease in humans. The prion particle consists mainly, if not entirely, of PrPSc, a posttranslationally modified isoform of the cellular host-encoded prion protein (PrPc). It has been suggested that additional cellular factors might be involved in the physiological function of PrPc and in the propagation of PrPSc. Here we employ a Saccharomyces cerevisiae two-hybrid screen to search for proteins which interact specifically with the Syrian golden hamster prion protein. Screening of a HeLa cDNA library identified heat shock protein 60 (Hsp60), a cellular chaperone as a major interactor for PrPc. The specificity of the interaction was confirmed in vitro for the recombinant proteins PrPc23-231 and rPrP27-30 fused to glutathione S-transferase with recombinant human Hsp60 as well as the bacterial GroEL. The interaction site for recombinant Hsp60 and GroEL proteins was mapped between amino acids 180 and 210 of the prion protein by screening with a set of recombinant PrPc fragments. The binding of Hsp60 and GroEL occurs within a region which contains parts of the putative alpha-helical domains H3 and H4 of the prion protein.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-1351721, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-1353761, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-1525471, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-1675487, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-1680859, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-1731198, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-1968466, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-2448875, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-2547163, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-2564438, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-271968, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-2873895, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-3112578, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-388439, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-4957205, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-4963878, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-6432339, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-6801762, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7518226, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7553876, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7609044, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7628468, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7703230, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7732006, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7754373, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7769698, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7773752, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7791905, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7902575, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7911805, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7913747, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7913989, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7916211, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7935790, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-7935796, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-8041623, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-8104185, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-8154865, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-8171010, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-8197133, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-8242750, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-8419912, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-8448158, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-8564353, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-8619803, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-9383397, http://linkedlifedata.com/resource/pubmed/commentcorrection/8676499-9383432
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4724-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Prion protein PrPc interacts with molecular chaperones of the Hsp60 family.
pubmed:affiliation
Laboratorium Für Molekulare Biologie-Genzentrum-Institute Für Biochemie der Ludwig-Maximilians-Universität Munchen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't