Effect of single point mutations in citrate synthase on binding to GroEL

FEBS Letters

Zahn, Ralph¹  Lindner, Peter¹  Axmann, Sabine E.¹  Plückthun, Andreas¹ 

[1] Biochemisches Institut, Universität Zürich, Winterthurerstr. 190, CH-8057 Zürich, Switzerland

关键词: Molecular chaperone;    Protein folding;    Protein stability;    GroEL;    Pre-β-lactamase;    Citrate synthase;    DTT;    dithiothreitol;    SDS;    sodium dodecyl sulfate;    CS;    citrate synthase;    Bla;    pre-β-lactamase;   

DOI  :  10.1016/0014-5793(96)00013-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Six single point mutants of yeast citrate synthase were analyzed for binding to the molecular chaperone GroEL. In contrast to the wild-type and G276S, all other G276-mutants were able to displace pre-β-lactamase from GroEL. The off-rate constant for pre-β-lactamase must be at least partially rate-limiting, leading to an equilibrium dissociation constant between 10⁻¹⁰ M and 10⁻¹²M. Direct evidence for binding of citrate synthase was obtained from gel filtration experiments. The results suggest that thermodynamic rather than structural features of the mutants determine the degree of binding to the chaperone.

【 授权许可】

Unknown