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 language | English |
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Pages (from-to) | 242-246 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 325 |
Issue number | 3 |
DOIs | |
State | Published - 5 Jul 1993 |
Keywords
- Calmodulin
- Saccharomyces cerevisiae
- UBC4
- Ubiquitin
- Ubiquitin protein ligase