{"database":"bioimages","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":[null],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-BIAD1181"],"repository":["bioimages"],"figure_sub":["Specimen","Image analysis","Study Component","organisation","Biosample","Associations","Image acquisition"],"pubmed_authors":["Cristina Gallego Páramo","Dina Schneidman-Duhovny","Maria de la Torre-Barranco","Regina Feederle","Juan Zou","Maria Alba Abad","Emilija Ruksenaite","Owen R. Davies","A. Arockia Jeyaprakash","Uhn-Soo Cho","Bethan Medina-Pritchard","Patrick Heun","Kazuma Shimanaka","Juri Rappsilber","Sang Ho Park","Reshma Reshma Thamkachy","Carla G. Chiodi"],"additional_accession":[]},"is_claimable":false,"name":"Structural Basis for Mis18 Complex Assembly: Implications for Centromere Maintenance ","description":"The centromere, defined by the enrichment of CENP-A (a Histone H3 variant) containing nucleosomes, is a specialised chromosomal locus that acts as a microtubule attachment site. To preserve centromere identity, CENP-A levels must be maintained through active CENP-A loading during the cell cycle. A central player mediating this process is the Mis18 complex (Mis18α, Mis18β and Mis18BP1), which recruits the CENP-A specific chaperone HJURP to centromeres for CENP-A deposition. Here, using a multi-pronged approach, we characterise the structure of the Mis18 complex and show that multiple hetero- and homo-oligomeric interfaces facilitate the hetero-octameric Mis18 complex assembly composed of 4 Mis18α, 2 Mis18β and 2 Mis18BP1. Evaluation of structure-guided/separation-of-function mutants reveals","dates":{"release":"2024-05-20T00:00:00Z","modification":"2024-05-20T11:38:25.015Z","creation":"2024-05-20T11:38:25.015Z"},"accession":"S-BIAD1181","cross_references":{}}