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J Biol Chem, Vol. 274, Issue 3, 1783-1790, January 15, 1999
From the Department of Biochemistry and Cell Biology, Institute for
Cell and Developmental Biology, SUNY Stony Brook, Stony Brook,
New York 11794-5215
The synaptonemal complex (SC) is a proteinaceous
structure formed between pairs of homologous chromosomes during
prophase I of meiosis. The proper assembly of axial elements (AEs),
lateral components of the SC, during meiosis in the yeast,
Saccharomyces cerevisiae, is essential for wild-type levels
of recombination and for the accurate segregation of chromosomes at the
first meiotic division. Genetic experiments have indicated that the
stoichiometry between two meiosis-specific components of AEs in
S. cerevisiae, HOP1 and RED1, is
critical for proper assembly and function of the SC. A third
meiosis-specific gene, MEK1, which encodes a putative serine/threonine protein kinase, is also important for proper AE
function, suggesting that AE formation is regulated by phosphorylation. In this paper, we demonstrate that Mek1p is a functional kinase in vitro and that catalytic activity is an essential part
of the meiotic function of Mek1 in vivo. Immunoblot
analysis revealed that Red1p is a
MEK1-dependent phosphoprotein.
Co-immunoprecipitation experiments demonstrated that the interaction
between Hop1p and Red1p is enhanced by the presence of
MEK1. Thus, MEK1-dependent phosphorylation of Red1p facilitates the formation of Hop1p/Red1p hetero-oligomers, thereby enabling the formation of functional AEs.
Red1p, a MEK1-dependent Phosphoprotein
That Physically Interacts with Hop1p during Meiosis in Yeast
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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