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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1998-7-28
pubmed:abstractText
Mechanisms to acquire tolerance against heat, an important environmental stress condition, have evolved in all organisms, but are largely unknown. When Saccharomyces cerevisiae cells are pre-conditioned at 37 degrees C, they survive an otherwise lethal exposure to 48-50 degrees C, and form colonies at 24 degrees C. We show here that incubation of yeast cells at 48-50 degrees C, after pre-conditioning at 37 degrees C, resulted in inactivation of exocytosis, and in conformational damage and loss of transport competence of proteins residing in the endoplasmic reticulum (ER). Soon after return of the cells to 24 degrees C, membrane traffic was resumed, but cell wall invertase, vacuolar carboxypeptidase Y and a secretory beta-lactamase fusion protein remained in the ER for different times. Thereafter their transport competence was resumed very slowly with widely varying kinetics. While the proteins were undergoing conformational repair in the ER, their native counterparts, synthesized after shift of the cells to 24 degrees C, folded normally, by-passed the heat-affected copies and exited rapidly the ER. The Hsp70 homolog Lhs1p was required for acquisition of secretion competence of heat-damaged proteins. ER retention and refolding of heat-denatured glycoproteins appear to be part of the cellular stress response.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:volume
111 ( Pt 11)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1575-82
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Transient ER retention as stress response: conformational repair of heat-damaged proteins to secretion-competent structures.
pubmed:affiliation
Yeast Laboratory, Institute of Biotechnology, PO Box 56, Finland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't