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

Research output: Contribution to journalArticlepeer-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 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.

Original languageEnglish
Pages (from-to)242-246
Number of pages5
JournalFEBS Letters
Volume325
Issue number3
DOIs
StatePublished - 5 Jul 1993

Keywords

  • Calmodulin
  • Saccharomyces cerevisiae
  • UBC4
  • Ubiquitin
  • Ubiquitin protein ligase

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