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Instruments / Technical Area	Publication Details	Published	Actions
I02-Macromolecular Crystallography	Structural basis for microtubule recognition by the human kinetochore Ska complex Maria Alba Abad , Bethan Medina , Anna Santamaria , Juan Zou , Carla Plasberg-Hill , Arumugam Madhumalar , Uma Jayachandran , Patrick Marc Redli , Juri Rappsilber , Erich A. Nigg , Jeyaprakash Arulanandam Nature Communications 5 DOI: 10.1038/ncomms3964 PMID: 24413531 Diamond Proposal Number(s): [7613, 9487] Open Access Show Abstract ▼ Abstract: The ability of kinetochores (KTs) to maintain stable attachments to dynamic microtubule structures (‘straight’ during microtubule polymerization and ‘curved’ during microtubule depolymerization) is an essential requirement for accurate chromosome segregation. Here we show that the kinetochore-associated Ska complex interacts with tubulin monomers via the carboxy-terminal winged-helix domain of Ska1, providing the structural basis for the ability to bind both straight and curved microtubule structures. This contrasts with the Ndc80 complex, which binds straight microtubules by recognizing the dimeric interface of tubulin. The Ska1 microtubule-binding domain interacts with tubulins using multiple contact sites that allow the Ska complex to bind microtubules in multiple modes. Disrupting either the flexibility or the tubulin contact sites of the Ska1 microtubule-binding domain perturbs normal mitotic progression, explaining the critical role of the Ska complex in maintaining a firm grip on dynamic microtubules.	Jan 2014
I03-Macromolecular Crystallography I04-1-Macromolecular Crystallography (fixed wavelength)	Structural basis for centromere maintenance by Drosophila CENP ‐A chaperone CAL 1 Bethan Medina-Pritchard , Vasiliki Lazou , Juan Zou , Olwyn Byron , Maria A. Abad , Juri Rappsilber , Patrick Heun , A. Arockia Jeyaprakash The Embo Journal 7 DOI: 10.15252/embj.2019103234 Open Access Show Abstract ▼ Abstract: Centromeres are microtubule attachment sites on chromosomes defined by the enrichment of histone variant CENP‐A‐containing nucleosomes. To preserve centromere identity, CENP‐A must be escorted to centromeres by a CENP‐A‐specific chaperone for deposition. Despite this essential requirement, many eukaryotes differ in the composition of players involved in centromere maintenance, highlighting the plasticity of this process. In humans, CENP‐A recognition and centromere targeting are achieved by HJURP and the Mis18 complex, respectively. Using X‐ray crystallography, we here show how Drosophila CAL1, an evolutionarily distinct CENP‐A histone chaperone, binds both CENP‐A and the centromere receptor CENP‐C without the requirement for the Mis18 complex. While an N‐terminal CAL1 fragment wraps around CENP‐A/H4 through multiple physical contacts, a C‐terminal CAL1 fragment directly binds a CENP‐C cupin domain dimer. Although divergent at the primary structure level, CAL1 thus binds CENP‐A/H4 using evolutionarily conserved and adaptive structural principles. The CAL1 binding site on CENP‐C is strategically positioned near the cupin dimerisation interface, restricting binding to just one CAL1 molecule per CENP‐C dimer. Overall, by demonstrating how CAL1 binds CENP‐A/H4 and CENP‐C, we provide key insights into the minimalistic principles underlying centromere maintenance.	Mar 2020

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