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A second Wpl1 anti‐cohesion pathway requires dephosphorylation of fission yeast kleisin Rad21 by PP 4
Author(s) -
Birot Adrien,
Eguienta Karen,
Vazquez Stéphanie,
Claverol Stéphane,
Bonneu Marc,
Ekwall Karl,
Javerzat JeanPaul,
Vaur Sabine
Publication year - 2017
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.201696050
Subject(s) - establishment of sister chromatid cohesion , cohesin , biology , chromatid , sister chromatids , chromosome segregation , phosphorylation , mutant , genetics , microbiology and biotechnology , dna , chromosome , chromatin , gene
Cohesin mediates sister chromatid cohesion which is essential for chromosome segregation and repair. Sister chromatid cohesion requires an acetyl‐transferase (Eso1 in fission yeast) counteracting Wpl1, promoting cohesin release from DNA . We report here that Wpl1 anti‐cohesion function includes an additional mechanism. A genetic screen uncovered that Protein Phosphatase 4 ( PP 4) mutants allowed cell survival in the complete absence of Eso1. PP 4 co‐immunoprecipitated Wpl1 and cohesin and Wpl1 triggered Rad21 de‐phosphorylation in a PP 4‐dependent manner. Relevant residues were identified and mapped within the central domain of Rad21. Phospho‐mimicking alleles dampened Wpl1 anti‐cohesion activity, while alanine mutants were neutral indicating that Rad21 phosphorylation would shelter cohesin from Wpl1 unless erased by PP 4. Experiments in post‐replicative cells lacking Eso1 revealed two cohesin populations. Type 1 was released from DNA by Wpl1 in a PP 4‐independent manner. Type 2 cohesin, however, remained DNA ‐bound and lost its cohesiveness in a manner depending on Wpl1‐ and PP 4‐mediated Rad21 de‐phosphorylation. These results reveal that Wpl1 antagonizes sister chromatid cohesion by a novel pathway regulated by the phosphorylation status of the cohesin kleisin subunit.