title: An acetyltransferase-independent function of Eso1 regulates centromere cohesion.
abstract: Eukaryotes contain three essential Structural Maintenance of Chromosomes (SMC) complexes: cohesin, condensin, and Smc5/6. Cohesin forms a ring-shaped structure that embraces sister chromatids to promote their cohesion. The cohesiveness of cohesin is promoted by acetylation of N-terminal lysines of the Smc3 subunit by the acetyltransferases Eco1 in Saccharomyces cerevisiae and the homologue, Eso1, in Schizosaccharomyces pombe. In both yeasts, these acetyltransferases are essential for cell viability. However, whereas nonacetylatable Smc3 mutants are lethal in S. cerevisiae, they are not in S. pombe We show that the lethality of a temperature-sensitive allele of eso1 (eso1-H17) is due to activation of the spindle assembly checkpoint (SAC) and is associated with premature centromere separation. The lack of cohesion at the centromeres does not correlate with Psm3 acetylation or cohesin levels at the centromeres, but is associated ith significantly reduced recruitment of the cohesin regulator Pds5. The SAC activation in this context is dependent on Smc5/6 function, which is required to remove cohesin from chromosome arms but not centromeres. The mitotic defects caused by Smc5/6 and Eso1 dysfunction are cosuppressed in double mutants. This identifies a novel function (or functions) for Eso1 and Smc5/6 at centromeres and extends the functional relationships between these SMC complexes.
authors: Department of Oncological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029.
authors: Su-Jiun
authors: SJ
authors: Lin
authors: Department of Oncological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029.
authors: Claudia
authors: C
authors: Tapia-Alveal
authors: Department of Genetics and Genomic Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029.
authors: Omar J
authors: OJ
authors: Jabado
authors: Department of Hematology and Oncology, Icahn School of Medicine at Mount Sinai, New York, NY 10029.
authors: Doris
authors: D
authors: Germain
authors: Department of Oncological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029 matthew.oconnell@mssm.edu.|Graduate School of Biomedical Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029.
authors: Matthew J
authors: MJ
authors: O'Connell
mesh_terms: D000123:Acetyltransferases / Q000235:genetics / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism / Q000502:physiology; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism*; D002503:Centromere / Q000201:enzymology*; D002842:Chromatids / Q000201:enzymology; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism; D020090:Chromosome Segregation; D015825:Chromosomes, Fungal / Q000201:enzymology; D004268:DNA-Binding Proteins / Q000378:metabolism / Q000502:physiology; D008938:Mitosis / Q000502:physiology; D046912:Multiprotein Complexes / Q000378:metabolism / Q000502:physiology; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism*; D016196:S Phase; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D012568:Schizosaccharomyces / Q000166:cytology / Q000201:enzymology; D029702:Schizosaccharomyces pombe Proteins / Q000235:genetics / Q000378:metabolism*; D000097722:Cohesins
chemical_list: D000123:Acetyltransferases; D000251:Adenosine Triphosphatases; D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D046912:Multiprotein Complexes; D009687:Nuclear Proteins; D029701:Saccharomyces cerevisiae Proteins; D029702:Schizosaccharomyces pombe Proteins; D000097722:Cohesins; C407842:Eso1 protein, S pombe; C108312:condensin complexes; C118076:ECO1 protein, S cerevisiae