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Glycosylation inhibits the interaction of invertase with the chaperone GroEL
Author(s) -
Kern Gunther,
Schmidt Marion,
Buchner Johannes,
Jaenicke Rainer
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80667-6
Subject(s) - groel , invertase , chaperone (clinical) , chemistry , biochemistry , protein folding , glycosylation , mannose , thermostability , saccharomyces cerevisiae , biophysics , enzyme , yeast , biology , escherichia coli , medicine , pathology , gene
During refolding and reassociation of chemically denatured non‐glycosylated invertase from Saccharomyces cerevisiae , aggregation competes with correct folding, leading to low yields of reactivation (Kern et al. (1992) Protein Sci. 1, 120–131). In the presence of the chaperone GroEL, refolding is completely arrested. This suggests the formation of a stable complex between GroEL and non‐native non‐glycosylated invertase. Addition of MgATP results in a slow release of active invertase from the chaperone complex. When GroEL/ES and MgATP are present during refolding, the final reactivation yield increases from 14% to 36%. In contrast, refolding of the core‐glycosylated and the high‐mannose glycosylated forms of invertase is not arrested by GroEL. Only a short lag phase at the beginning of reactivation and a slightly increased reactivation yield (64% to 86% for core‐glycosylated and 62% to 76% for external invertase) indicate a weak interaction of the glycosylated forms with the chaperone.