Chaperone effects on prion and nonprion aggregates. / Rikhvanov, Eugene G.; Romanova, Nina V.; Chernoff, Yury O.
Protein-Based Inheritance. Taylor & Francis, 2007. p. 83-92.Research output: Chapter in Book/Report/Conference proceeding › Chapter › Research › peer-review
}
TY - CHAP
T1 - Chaperone effects on prion and nonprion aggregates
AU - Rikhvanov, Eugene G.
AU - Romanova, Nina V.
AU - Chernoff, Yury O.
PY - 2007/1/1
Y1 - 2007/1/1
N2 - Exposure to high temperature or other stresses induces a synthesis of heat shock proteins. Many of these proteins are molecular chaperones, and some of them help cells to cope with heat-induced denaturation and aggregation of other proteins. In the last decade, chaperones have received increased attention in connection with their role in maintenance and propagation of the Saccharomyces cerevisiae prions, infectious or heritable agents transmitted at the protein level. Recent data suggest that functioning of the chaperones in reactivation of heat-damaged proteins and in propagation of prions is based on the same molecular mechanisms but may lead to different consequences depending on the type of aggregate. In both cases the conceited and balanced action of “chaperones’ team”, including Hsp 104, Hsp70, Hsp40 and possibly other proteins, determines whether a misfolded protein is to be incorporated into an aggregate, rescued to the native state or targeted for degradation.
AB - Exposure to high temperature or other stresses induces a synthesis of heat shock proteins. Many of these proteins are molecular chaperones, and some of them help cells to cope with heat-induced denaturation and aggregation of other proteins. In the last decade, chaperones have received increased attention in connection with their role in maintenance and propagation of the Saccharomyces cerevisiae prions, infectious or heritable agents transmitted at the protein level. Recent data suggest that functioning of the chaperones in reactivation of heat-damaged proteins and in propagation of prions is based on the same molecular mechanisms but may lead to different consequences depending on the type of aggregate. In both cases the conceited and balanced action of “chaperones’ team”, including Hsp 104, Hsp70, Hsp40 and possibly other proteins, determines whether a misfolded protein is to be incorporated into an aggregate, rescued to the native state or targeted for degradation.
UR - http://www.scopus.com/inward/record.url?scp=77952019194&partnerID=8YFLogxK
U2 - 10.1201/9781498712507-13
DO - 10.1201/9781498712507-13
M3 - Chapter
SN - 9781587061387
SP - 83
EP - 92
BT - Protein-Based Inheritance
PB - Taylor & Francis
ER -
ID: 49545569