Unknown

Dataset Information

0

Acetylation regulates monopolar attachment at multiple levels during meiosis I in fission yeast.


ABSTRACT: In fission yeast, meiotic mono-orientation of sister kinetochores is established by cohesion at the core centromere, which is established by a meiotic cohesin complex and the kinetochore protein Moa1. The cohesin subunit Psm3 is acetylated by Eso1 and deacetylated by Clr6. We show that in meiosis, Eso1 is required for establishing core centromere cohesion during S phase, whereas Moa1 is required for maintaining this cohesion after S phase. The clr6-1 mutation suppresses the mono-orientation defect of moa1? cells, although the Clr6 target for this suppression is not Psm3. Thus, several acetylations are crucial for establishing and maintaining core centromere cohesion.

SUBMITTER: Kagami A 

PROVIDER: S-EPMC3207105 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Acetylation regulates monopolar attachment at multiple levels during meiosis I in fission yeast.

Kagami Ayano A   Sakuno Takeshi T   Yamagishi Yuya Y   Ishiguro Tadashi T   Tsukahara Tatsuya T   Shirahige Katsuhiko K   Tanaka Koichi K   Watanabe Yoshinori Y  

EMBO reports 20111028 11


In fission yeast, meiotic mono-orientation of sister kinetochores is established by cohesion at the core centromere, which is established by a meiotic cohesin complex and the kinetochore protein Moa1. The cohesin subunit Psm3 is acetylated by Eso1 and deacetylated by Clr6. We show that in meiosis, Eso1 is required for establishing core centromere cohesion during S phase, whereas Moa1 is required for maintaining this cohesion after S phase. The clr6-1 mutation suppresses the mono-orientation defe  ...[more]

Similar Datasets

| S-EPMC4612672 | biostudies-literature
2006-09-23 | GSE4792 | GEO
| S-EPMC3350546 | biostudies-literature
| S-EPMC3399777 | biostudies-literature
| S-EPMC4934050 | biostudies-literature
2010-06-10 | E-GEOD-4792 | biostudies-arrayexpress
| S-EPMC2526688 | biostudies-literature
| S-EPMC2172399 | biostudies-literature