SELECTIVE UBIQUITINATION OF CALMODULIN BY UBC4 AND A PUTATIVE UBIQUITIN PROTEIN LIGASE (E3) FROM SACCHAROMYCES-CEREVISIAE

被引：16

作者：

PARAG, HA ^{[1
]}

DIMITROVSKY, D ^{[1
]}

RABOY, B ^{[1
]}

KULKA, RG ^{[1
]}

机构：

[1] HEBREW UNIV JERUSALEM, ALEXANDER SILBERMAN INST LIFE SCI, DEPT BIOL CHEM, IL-91904 JERUSALEM, ISRAEL

来源：

FEBS LETTERS | 1993年 / 325卷 / 03期

基金：

以色列科学基金会;

关键词：

UBIQUITIN; CALMODULIN; UBC4; UBIQUITIN PROTEIN LIGASE; SACCHAROMYCES-CEREVISIAE;

D O I：

10.1016/0014-5793(93)81081-A

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A putative ubiquitin protein ligase (E3-CaM) which cooperates with UBC4 in selectively ubiquitinating calmodulin has been partially purified from Saccharomyces cerevisiae. Ca2+ was required for this activity and monoubiquitinated calmodulin was the main product of the reaction. The apparent K(m) of E3-CaM for calmodulin was approximately 1 muM which is of the same order of magnitude as the concentration of calmodulin in yeast cells. Proteins which are good substrates for other E3s (E3alpha or E3-R) were not ubiquitinated by E3-CaM. Lower but significant activities of E3-CaM were observed when UBC1 replaced UBC4.

引用

页码：242 / 246

页数：5

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