Characterization of the cullin and F‐box protein partner Skp1

FEBS Letters

Ng, Raymond W.M.¹  Yam, Cain H.¹  Lau, Anita W.S.¹  Poon, Randy Y.C.¹  Arooz, Talha¹  Chan, Iris W.Y.¹ 

[1] Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China

关键词: Cell cycle;    Cyclin;    Cyclin-dependent kinase;    Degradation;    Ubiquitination;    BSA;    bovine serum albumin;    CDK;    cyclin-dependent kinase;    GSH;    glutathione;    GST;    glutathione-S-transferase;    H6;    hexa-histidine;    PAGE;    polyacrylamide gel electrophoresis;    PCR;    polymerase chain reaction;    TCA;    trichloroacetic acid;   

DOI  :  10.1016/S0014-5793(98)01299-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Skp1 interacts with cullins, F-box containing proteins, and forms a complex with cyclin A-Cdk2 in mammalian cells. Skp1 is also involved in diverse biological processes like degradation of key cell cycle regulators, glucose sensing, and kinetochore function. However, little is known about the structure and exact function of Skp1. Here we characterized the interaction between Skp1 and the F-box protein Skp2. We show that Skp1 can bind to Skp2 in vitro using recombinant proteins, and in vivo using the yeast two-hybrid system. Deletion analysis of Skp1 indicated that most of the Skp1 protein is required for binding to Skp2. In mammalian cell extracts, a large portion of Skp1 appears to associate with proteins other than Skp2. Biochemical analysis indicated that Skp1 is likely to be a flexible, non-spherical protein, and is capable of forming dimers.

【 授权许可】

Unknown