title: Members of the NAP/SET family of proteins interact specifically with B-type cyclins.
abstract: Cyclin-dependent kinase complexes that contain the same catalytic subunit are able to induce different events at different times during the cell cycle, but the mechanisms by which they do so remain largely unknown. To address this problem, we have used affinity chromatography to identify proteins that bind specifically to mitotic cyclins, with the goal of finding proteins that interact with mitotic cyclins to carry out the events of mitosis. This approach has led to the identification of a 60-kD protein called NAP1 that interacts specifically with members of the cyclin B family. This interaction has been highly conserved during evolution: NAP1 in the Xenopus embryo interacts with cyclins B1 and B2, but not with cyclin A, and the S. cerevisiae homolog of NAP1 interacts with Clb2 but not with Clb3. Genetic experiments in budding yeast indicate that NAP1 plays an important role in the function of Clb2, while biochemical experiments demonstrate that purified NAP1 can be phosphorylated by cyclin B/p34cdc2 kinase complexes, but not by cyclin A/p34cdc2 kinase complexes. These results suggest that NAP1 is a protein involved in the specific functions of cyclin B/p34cdc2 kinase complexes. In addition to NAP1, we found a 43-kD protein in Xenopus that is homologous to NAP1 and also interacts specifically with B-type cyclins. This protein is the Xenopus homolog of the human SET protein, which was previously identified as part of a putative oncogenic fusion protein (Von Lindern et al., 1992).
authors.affiliation: Department of Physiology, University of California, San Francisco 94143-0444, USA.
authors.forename: D R
authors.initials: DR
authors.lastname: Kellogg
authors.forename: A
authors.initials: A
authors.lastname: Kikuchi
authors.forename: T
authors.initials: T
authors.lastname: Fujii-Nakata
authors.forename: C W
authors.initials: CW
authors.lastname: Turck
authors.forename: A W
authors.initials: AW
authors.lastname: Murray
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D016203:CDC2 Protein Kinase / Q000378:metabolism; D002451:Cell Compartmentation; D018797:Cell Cycle Proteins; D002846:Chromatography, Affinity; D002868:Chromosomal Proteins, Non-Histone; D019926:Cyclin B; D016213:Cyclins / Q000378:metabolism*; D003593:Cytoplasm / Q000737:chemistry; D004268:DNA-Binding Proteins; D056488:Histone Chaperones; D008938:Mitosis / Q000502:physiology*; D008969:Molecular Sequence Data; D009687:Nuclear Proteins; D056490:Nucleosome Assembly Protein 1; D010766:Phosphorylation; D011485:Protein Binding; D011506:Proteins / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors; D014981:Xenopus / Q000196:embryology / Q000378:metabolism
chemical_list: C093749:CLB2 protein, S cerevisiae; D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D019926:Cyclin B; D016213:Cyclins; D004268:DNA-Binding Proteins; D056488:Histone Chaperones; C533556:NAP1 protein, S cerevisiae; C533557:NAP1L1 protein, human; D009687:Nuclear Proteins; D056490:Nucleosome Assembly Protein 1; D011506:Proteins; C513473:SET protein, human; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D016203:CDC2 Protein Kinase