Glycosylation inhibits the interaction of invertase with the chaperone GroEL

FEBS Letters

Schmidt, Marion¹  Jaenicke, Rainer¹  Kern, Gunther¹  Buchner, Johannes¹ 

[1] Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Universitätsstraße 31, D-8400 Regensburg, Germany

关键词: Chaperone;    GroE;    Folding;    Aggregation;    Glycosylation;    Invertase;   

DOI  :  10.1016/0014-5793(92)80667-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown