search

pombase / curation

PomBase curation
7 stars 0 forks source link

CENP-A loading #3357

Open ValWood opened 2 years ago

ValWood commented 2 years ago

Since CENP-A is not loaded in mitosis, it should be possible to add "during_interphase" to all of these. https://www.pombase.org/term/GO:0034080

ValWood commented 2 years ago

The timing of CENP-A deposition differs between organisms, occurring in the early G1 phase in humans as opposed to mainly in G2 in fission yeast6,7.

Lando, D. et al. Quantitative single-molecule microscopy reveals that CENP- ACnp1 deposition occurs during G2 in fission yeast. Open Biol. 2, 120078 (2012).

ValWood commented 2 years ago

The Mis18 complex and Scm3 localise to kine- tochores during interphase but are dispersed during mitosis, whereas Mis6 remains throughout the cell cycle9,15,16,36.

9 Hayashi, T. et al. Mis16 and Mis18 are required for CENP-A loading and histone deacetylation at centromeres. Cell 118, 715–729 (2004). 15 Williams, J. S., Hayashi, T., Yanagida, M. & Russell, P. Fission yeast Scm3 mediates stable assembly of Cnp1/CENP-A into centromeric chromatin. Mol. Cell 33, 287–298 (2009). 16 Pidoux, A. L. et al. Fission yeast Scm3: A CENP-A receptor required for integrity of subkinetochore chromatin. Mol. Cell 33, 299–311 (2009). 36 Saitoh, S., Takahashi, K. & Yanagida, M. Mis6, a fission yeast inner centromere protein, acts during G1/S and forms specialized chromatin required for equal segregation. Cell 90, 131–143 (1997).

ValWood commented 2 years ago

prioritise Hayashi for full curation

Screenshot 2022-10-06 at 10 57 21
ValWood commented 2 years ago

Also: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6677171/ Centromeric chromatin in fission yeast is distinguished by the presence of nucleosomes containing the histone H3 variant Cnp1CENP-A. Cell cycle–specific deposition of Cnp1 requires the Mis16–Mis18–Mis19 complex, which is thought to direct recruitment of Scm3-chaperoned Cnp1/histone H4 dimers to DNA. Here, we present the structure of the essential Mis18 partner protein Mis19 and describe its interaction with Mis16, revealing a bipartite-binding site. We provide data on the stoichiometry and overall architecture of the complex and provide detailed insights into the Mis18–Mis19 interface.

ValWood commented 2 years ago

need https://github.com/geneontology/go-ontology/issues/24147 before proceeding