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PMID: 7622566 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Members of the NAP/SET family of proteins interact specifically with B-type cyclins.

The Journal of cell biology ·Vol. 130 ·No. 3 ·1995-08-00 ·Pages 661-73

Kellogg DR, Kikuchi A, Fujii-Nakata T, Turck CW, Murray AW

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).

MeSH Terms
Amino Acid Sequence Animals Base Sequence CDC2 Protein Kinase/metabolism Cell Compartmentation Cell Cycle Proteins Chromatography, Affinity Chromosomal Proteins, Non-Histone Cyclin B Cyclins/metabolism Cytoplasm/chemistry DNA-Binding Proteins Histone Chaperones Mitosis/physiology Molecular Sequence Data Nuclear Proteins Nucleosome Assembly Protein 1 Phosphorylation Protein Binding Proteins/genetics,metabolism Saccharomyces cerevisiae/metabolism Saccharomyces cerevisiae Proteins Sequence Homology, Amino Acid Transcription Factors Xenopus/embryology,metabolism
Chemicals
CLB2 protein, S cerevisiae Cell Cycle Proteins Chromosomal Proteins, Non-Histone Cyclin B Cyclins DNA-Binding Proteins Histone Chaperones NAP1 protein, S cerevisiae NAP1L1 protein, human Nuclear Proteins Nucleosome Assembly Protein 1 Proteins SET protein, human Saccharomyces cerevisiae Proteins Transcription Factors CDC2 Protein Kinase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Kellogg D R
Department of Physiology, University of California, San Francisco 94143-0444, USA.
Kikuchi A
Fujii-Nakata T
Turck C W
Murray A W
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.130.3.661
Published
1995-08-00
Pages
661-73
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2120524
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.130.3.661 PMC Full Text View journal details
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