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Oligomerization state in solution of the cell cycle regulators p13 suc1 from the fission yeast and p9 cksphy from the myxomycete Physarum , two members of the cks family
Author(s) -
Birck Catherine,
Raynaud-Messina Brigitte,
Samamaa Jean-Pierre
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00300-x
Subject(s) - physarum , cyclin dependent kinase 1 , yeast , physarum polycephalum , protein subunit , biology , complementation , gene product , cell cycle protein , schizosaccharomyces pombe , cell cycle , biochemistry , gene , microbiology and biotechnology , saccharomyces cerevisiae , gene expression , phenotype
The cks proteins (for cdc2 kinase subunit) are essential cell cycle regulators. They interact strongly with the mitotic cdc2 kinase, but the mechanism and the biological function of this association still await understanding. The oligomerization state in solution of two members of this ubiquitous protein family, the sucl gene product from the fission yeast and the newly cloned cksphy gene product from the myxomycete Physarum , was investigated by small‐angle X‐ray scattering (SAXS) and biochemical methods. We found that the major molecular species are monodispersed monomeric proteins. Minor amounts of dimeric sucl proteins were also found, but no equilibrium between the two forms was observed and surprisingly, the hexameric assemblies observed in the crystal structure of the human ckshs2 homolog were not detected. These apparent discrepancies between proteins that display cross‐complementation address the question of the control of the cks oligomerization process and its link to the biological function.