Mass Spectrometric Analysis of the Anaphase-Promoting Complex from Yeast: Identification of a Subunit Related to Cullins

Author:

Zachariae Wolfgang123,Shevchenko Andrej123,Andrews Paul D.123,Ciosk Rafael123,Galova Marta123,Stark Michael J. R.123,Mann Matthias123,Nasmyth Kim123

Affiliation:

1. W. Zachariae, R. Ciosk, M. Galova, K. Nasmyth, Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria.

2. A. Shevchenko and M. Mann, European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69012 Heidelberg, Germany.

3. P. D. Andrews and M. J. R. Stark, Department of Biochemistry, University of Dundee, Dundee DD1 4HN, UK.

Abstract

Entry into anaphase and exit from mitosis depend on a ubiquitin–protein ligase complex called the anaphase-promoting complex (APC) or cyclosome. At least 12 different subunits were detected in the purified particle from budding yeast, including the previously identified proteins Apc1p, Cdc16p, Cdc23p, Cdc26p, and Cdc27p. Five additional subunits purified in low nanogram amounts were identified by tandem mass spectrometric sequencing. Apc2p, Apc5p, and the RING-finger protein Apc11p are conserved from yeast to humans. Apc2p is similar to the cullin Cdc53p, which is a subunit of the ubiquitin–protein ligase complex SCF Cdc4 required for the initiation of DNA replication.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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