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H, 13C and 15N resonance assignments for the microtubule‑binding domain of the kinetoplastid kinetochore protein KKT4 from Trypanosoma brucei Patryk Ludzia1 · Bungo Akiyoshi1 · Christina Redfield1  Received: 22 May 2020 / Accepted: 6 July 2020 © The Author(s) 2020

Abstract KKT4 is a kinetoplastid-specific microtubule-binding kinetochore protein that lacks significant similarity to any known kinetochore or microtubule-binding proteins. Here we present the 1H, 13C and 15N resonance assignments for several fragments from the microtubule-binding domain of KKT4 ­(KKT4115–343) from Trypanosoma brucei. These assignments provide the starting point for detailed investigations of the structure, dynamics and interactions of the microtubule-binding region of KKT4. Keywords  KKT4 · Kinetoplastid · Kinetochore · Trypanosomes · NMR resonance assignments

Biological context During chromosome segregation, cells must accurately transmit their genetic material into two daughter cells in an organised manner. Errors in this process lead to genetic abnormalities that can lead to cancer or cell death. Chromosome segregation is therefore a critical requirement for the survival and development of all organisms (McIntosh 2016). In eukaryotes, a key structure involved in this process is the kinetochore, a dynamic protein complex that assembles onto centromeric DNA of each chromosome and captures spindle microtubules (Brinkley and Stubblefield 1966; Cheeseman 2014). Many kinetochore components, such as CENP-A and Ndc80, are widely conserved among eukaryotes (Biggins 2013; Cheeseman and Desai 2008; Meraldi et al. 2006; Santaguida and Musacchio 2009; van Hooff et al. 2017) and it

Electronic supplementary material  The online version of this article (https​://doi.org/10.1007/s1210​4-020-09968​-1) contains supplementary material, which is available to authorized users. * Bungo Akiyoshi [email protected] * Christina Redfield [email protected] 1



Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK

was thought that all eukaryotes utilise the same set of kinetochore proteins. However, none of the canonical kinetochore proteins has been found in kinetoplastids, an evolutionarily divergent group of unicellular flagellated eukaryotes including parasitic trypanosomatids (e.g. Trypanosoma brucei, Trypanosoma cruzi, and Leishmania species). Instead, a number of unique kinetochore proteins, KKT1–25 and KKIP1–12, were identified in T. brucei (Akiyoshi 2016; Akiyoshi and Gull 2014; Brusini et al. 2019; D’Archivio and Wickstead 2017; Nerusheva and Akiyoshi 2016; Nerusheva et al. 2019). No significant similarity to conventional kinetochore proteins is found in these proteins and very little is known about their structure, function and interactions. We recently showed that the KKT4 protein, and in particular a fragment containing residues 115–343, has microtubule-binding activities in vitro (Llauro et al. 2018). Further investigation demonstrated that KKT4 can track depolymerising m

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