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Characterisation of human cdc2 lysine 33 mutations expressed in the fission yeast Schizosaccharomyces pombe
Author(s) -
Leroy Dorothée,
Birck Catherine,
Brambilla Paolo,
Samama Jean-Pierre,
Ducommun Bernard
Publication year - 1996
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)01514-0
Subject(s) - schizosaccharomyces pombe , cyclin dependent kinase 1 , yeast , schizosaccharomyces , mutant , biology , biochemistry , saccharomyces cerevisiae , cell cycle , chemistry , microbiology and biotechnology , cell , gene
The mammalian p34 cdc2 protein kinase, a universal cell cycle regulator, complements cdc2/CDC28 temperature‐sensitive mutations in yeasts. We report the biochemical characterisation of two substitutions of human cdc2 at lysine 33, a residue involved in nucleotide binding, that differently alter the fission yeast cell cycle. K33A‐hscdc2 and K33R‐hscdc2 mutants are both catalytically inactive, but overexpression of K33R‐cdc2 is lethal while K33A‐cdc2 is not. We show that human K33R‐cdc2 acts as a dominant negative allele that associates yeast cdc13/cyclinB and therefore renders endogeneous Schizosaccharomyces pombe cdc2 unactivatable. These results are discussed on the light of the molecular modeling of the mutants in the cdc2 model structure.