TY - JOUR
T1 - Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones
AU - Ben-Zvi, Anat Peres
AU - Goloubinoff, Pierre
PY - 2002/12/20
Y1 - 2002/12/20
N2 - External stresses or mutations may cause labile proteins to lose their distinct native conformations and seek alternatively stable aggregated forms. Molecular chaperones that specifically act on protein aggregates were used here as a tool to address the biochemical nature of stable homo- and hetero-aggregates from non-pathogenic proteins formed by heat-stress. Confirmed by sedimentation and activity measurements, chaperones demonstrated that a single polypeptide chain can form different species of aggregates, depending on the denaturing conditions. Indicative of a cascade reaction, sub-stoichiometric amounts of one fast-aggregating protein strongly accelerated the conversion of another soluble, slow-aggregating protein into insoluble, chaperone-resistant aggregates. Chaperones strongly inhibited seed-induced protein aggregation, suggesting that they can prevent and cure proteinaceous infectious behavior in homo- and hetero-aggregates from common and disease-associated proteins in the cell.
AB - External stresses or mutations may cause labile proteins to lose their distinct native conformations and seek alternatively stable aggregated forms. Molecular chaperones that specifically act on protein aggregates were used here as a tool to address the biochemical nature of stable homo- and hetero-aggregates from non-pathogenic proteins formed by heat-stress. Confirmed by sedimentation and activity measurements, chaperones demonstrated that a single polypeptide chain can form different species of aggregates, depending on the denaturing conditions. Indicative of a cascade reaction, sub-stoichiometric amounts of one fast-aggregating protein strongly accelerated the conversion of another soluble, slow-aggregating protein into insoluble, chaperone-resistant aggregates. Chaperones strongly inhibited seed-induced protein aggregation, suggesting that they can prevent and cure proteinaceous infectious behavior in homo- and hetero-aggregates from common and disease-associated proteins in the cell.
UR - http://www.scopus.com/inward/record.url?scp=0037147221&partnerID=8YFLogxK
U2 - 10.1074/jbc.M209163200
DO - 10.1074/jbc.M209163200
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C2 - 12377766
AN - SCOPUS:0037147221
SN - 0021-9258
VL - 277
SP - 49422
EP - 49427
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 51
ER -