Abstract
Cohesion between sister chromatids occurs along the length of chromosomes, where it plays essential roles in chromosome segregation. We show here that the centromere, a cis-acting cohesion factor, directs the binding of Mcd1p, a cohesin subunit, to at least 2 kb regions flanking centromeres in a sequence-independent manner. The centromere is essential for the maintenance as well as the establishment of this cohesin domain. The efficiency of Mcd1p binding within the cohesin domain is independent of the primary nucleotide sequence of the centromere-flanking DNA but correlates with high A + T DNA content. Thus, the function of centromeres in the cohesion of centromere-proximal regions may be analogous to that of enhancers, nucleating cohesin complex binding over an extended chromosomal domain of A + T-rich DNA.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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AT Rich Sequence
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Binding Sites
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Cell Cycle Proteins / metabolism*
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Centromere / metabolism*
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Chromatids / metabolism*
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Chromatin / isolation & purification
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Chromosomal Proteins, Non-Histone
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Chromosomes, Fungal / metabolism
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Cohesins
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DNA Nucleotidyltransferases / metabolism
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DNA-Binding Proteins*
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Fungal Proteins / metabolism
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Nuclear Proteins / metabolism*
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Phosphoproteins
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Polymerase Chain Reaction
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Precipitin Tests
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Protein Binding
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Recombination, Genetic
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae Proteins*
Substances
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Cell Cycle Proteins
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Chromatin
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Chromosomal Proteins, Non-Histone
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DNA-Binding Proteins
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Fungal Proteins
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MCD1 protein, S cerevisiae
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MIF2 protein, S cerevisiae
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Nuclear Proteins
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Phosphoproteins
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Saccharomyces cerevisiae Proteins
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DNA Nucleotidyltransferases
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R recombinase