Selective ubiquitination of calmodulin by UBC4 and a putative ubiquitin protein ligase (E3) from Saccharomyces cerevisiae

Hadas A. Parag; Deborah Dimitrovsky; Bilha Raboy; Richard G. Kulka

doi:10.1016/0014-5793(93)81081-A

Selective ubiquitination of calmodulin by UBC4 and a putative ubiquitin protein ligase (E3) from Saccharomyces cerevisiae

Hadas A. Parag
, Deborah Dimitrovsky
, Bilha Raboy
, Richard G. Kulka^*

^*Corresponding author for this work

Alexander Silberman Institute of Life Sciences

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

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 μM which is of the same order of magnitude as the concentration of calmodulin in yeast cells. Proteins which are good substrates for other E3s (E3α or E3-R) were not ubiquitinated by E3-CaM. Lower but significant activities of E3-CaM were observed when UBC1 replaced UBC4.

Original language	English
Pages (from-to)	242-246
Number of pages	5
Journal	FEBS Letters
Volume	325
Issue number	3
DOIs	https://doi.org/10.1016/0014-5793(93)81081-A
State	Published - 5 Jul 1993

Keywords

Calmodulin
Saccharomyces cerevisiae
UBC4
Ubiquitin
Ubiquitin protein ligase

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10.1016/0014-5793(93)81081-A

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title = "Selective ubiquitination of calmodulin by UBC4 and a putative ubiquitin protein ligase (E3) from Saccharomyces cerevisiae",

abstract = "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 Km of E3-CaM for calmodulin was approximately 1 μM which is of the same order of magnitude as the concentration of calmodulin in yeast cells. Proteins which are good substrates for other E3s (E3α or E3-R) were not ubiquitinated by E3-CaM. Lower but significant activities of E3-CaM were observed when UBC1 replaced UBC4.",

keywords = "Calmodulin, Saccharomyces cerevisiae, UBC4, Ubiquitin, Ubiquitin protein ligase",

author = "Parag, \{Hadas A.\} and Deborah Dimitrovsky and Bilha Raboy and Kulka, \{Richard G.\}",

year = "1993",

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T1 - Selective ubiquitination of calmodulin by UBC4 and a putative ubiquitin protein ligase (E3) from Saccharomyces cerevisiae

AU - Parag, Hadas A.

AU - Dimitrovsky, Deborah

AU - Raboy, Bilha

AU - Kulka, Richard G.

PY - 1993/7/5

Y1 - 1993/7/5

N2 - 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 Km of E3-CaM for calmodulin was approximately 1 μM which is of the same order of magnitude as the concentration of calmodulin in yeast cells. Proteins which are good substrates for other E3s (E3α or E3-R) were not ubiquitinated by E3-CaM. Lower but significant activities of E3-CaM were observed when UBC1 replaced UBC4.

AB - 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 Km of E3-CaM for calmodulin was approximately 1 μM which is of the same order of magnitude as the concentration of calmodulin in yeast cells. Proteins which are good substrates for other E3s (E3α or E3-R) were not ubiquitinated by E3-CaM. Lower but significant activities of E3-CaM were observed when UBC1 replaced UBC4.

KW - Calmodulin

KW - Saccharomyces cerevisiae

KW - UBC4

KW - Ubiquitin

KW - Ubiquitin protein ligase

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JO - FEBS Letters

JF - FEBS Letters

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ER -

Selective ubiquitination of calmodulin by UBC4 and a putative ubiquitin protein ligase (E3) from Saccharomyces cerevisiae

Abstract

Keywords

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