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A Monoclonal Antibody Against the PSTAIR Sequence of p34 cdc2 , Catalytic Subunit of Maturation‐Promoting Factor and Key Regulator of the Cell Cycle
Author(s) -
Yamashita Masakane,
Yoshikuni Michiyasu,
Hirai Toshiaki,
Fukada Sachiko,
Nagahama Yoshitaka
Publication year - 1991
Publication title -
development, growth and differentiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.864
H-Index - 66
eISSN - 1440-169X
pISSN - 0012-1592
DOI - 10.1111/j.1440-169x.1991.00617.x
Subject(s) - cyclin dependent kinase 1 , biology , schizosaccharomyces pombe , biochemistry , protein subunit , cyclin dependent kinase complex , protein kinase a , cyclin dependent kinase , microbiology and biotechnology , cell cycle , kinase , cyclin dependent kinase 2 , yeast , gene , saccharomyces cerevisiae
A homolog of the serine/threonine protein kinase (p34 cdc2 ), encoded by the cdc2 + gene of the fission yeast ( Schizosaccharomyces pombe ), is a catalytic subunit of maturation‐promoting factor and a key regulator of the cell cycle. We have raised a monoclonal antibody against the most conserved amino acid sequence, the PSTAIR sequence (EGVPSTAIREISLLKE) of p34 cdc2 This antibody recognizes 31–34 kDa proteins by immunoblotting in all species examined so far. The proteins recognized by the anti‐PSTAIR antibody are probably either p34 cdc2 itself or proteins highly homologous to p34 cdc2 in the given species, since, in all species studies to date, they are all precipitated with p13 suc1 , the fission yeast suc 1 + gene product, which binds to p34 cdc2 with high specificity. The anti‐PSTAIR immunoprecipitate had no histone H1 kinase activity and did not contain cyclin B, suggesting that the PSTAIR region is masked when p34 cdc2 forms a complex with cyclin B as an active kinase. Immunoblotting with the anti‐PSTAIR antibody demonstrated that the fastest‐migrating form of p34 cdc2 homologues becomes abundant, when oocytes mature or the cell enters M phase. The possible significance of this observation is discussed in relation to the phosphorylation and activity state of p34 cdc2 The observed broad cross‐reactivity of the anti‐PSTAIR antibody against p34 cdc2 homologues in various species should permit us to examine the role of p34 cdc2 homologues in the regulation of the cell cycle in a variety of organisms.