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Mass spectrometric analysis of the anaphase-promoting complex from yeast: identification of a subunit related to cullins.

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 SCFCdc4 required for the initiation of DNA replication.

Pubmed ID: 9469814

Authors

  • Zachariae W
  • Shevchenko A
  • Andrews PD
  • Ciosk R
  • Galova M
  • Stark MJ
  • Mann M
  • Nasmyth K

Journal

Science (New York, N.Y.)

Publication Data

February 20, 1998

Associated Grants

None

Mesh Terms

  • Amino Acid Sequence
  • Anaphase
  • Anaphase-Promoting Complex-Cyclosome
  • Animals
  • Cell Cycle Proteins
  • Cullin Proteins
  • Cyclins
  • DNA Replication
  • Fungal Proteins
  • Genes, Fungal
  • Humans
  • Ligases
  • Mass Spectrometry
  • Molecular Sequence Data
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Sequence Alignment
  • Spindle Apparatus
  • Ubiquitin-Protein Ligase Complexes
  • Ubiquitin-Protein Ligases
  • Ubiquitins