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Covalent conjugation of mammalian calmodulin with ubiquitin
Author(s) -
Ziegenhagen R.,
Gehrke P.,
Jennissen H.P.
Publication year - 1988
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(88)80180-7
Subject(s) - calmodulin , ubiquitin , conjugate , biochemistry , chemistry , covalent bond , cytosol , ubiquitin conjugating enzyme , ubiquitin ligase , enzyme , biology , mathematical analysis , mathematics , organic chemistry , gene
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 Ca 2+ in the range of ∼10 μM for ubiquitination of calmodulin to occur. This novel conjugate (uCaM) shows a Ca 2+ ‐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.