Covalent conjugation of mammalian calmodulin with ubiquitin

FEBS Letters

Ziegenhagen, R.¹  Jennissen, H.P.¹  Gehrke, P.¹ 

[1] Institut für Physiologie, Physiologische Chemie & Ernährungsphysiologie, Ludwig-Maximilians-Universität München, Veterinärstr. 13, D-8000 München 22, FRG

关键词: Calmodulin;    Ubiquitin;    Calmodulin-ubiquitin conjugate;    Protein ubiquitination;    ATP-dependent proteolysis;    Trimethyllysine;   

DOI  :  10.1016/0014-5793(88)80180-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In this paper it is shown that mammalian calmodulin from bovine testis is a substrate for reticulocyte ubiquitin conjugating activity (UCA) forming a 1:1 covalent conjugate between bovine calmodulin and ubiquitin (uCaM). There is an absolute requirement for Ca²⁺ in the range of ∼10 μM for ubiquitination of calmodulin to occur. This novel conjugate (uCaM) shows a Ca²⁺-dependent mobility change in polyacrylamide gel electrophoresis in the presence of SDS, indicating that the calmodulin-ubiquitin conjugate still retains the mobility change of native calmodulin. This conjugation reaction could be of prime importance for the intracellular turnover of calmodulin in the mammalian cell, although it cannot be excluded that the ubiquitin-calmodulin conjugate might in itself be of biological relevance.

【 授权许可】

Unknown