The Terminin is a multiprotein complex composed of the proteins including Moidiliani (Moi), Verochio (Ver), HP1-ORC Associating Protein (HOAP), Separase (Sse) and a variety of other important proteins, most localized strictly at the telomeres. This multiprotein complex is responsible for the capping of telomeres and the prevention of telomeric fusions. Recently, Sse, a fly protein that has a human homologue, has been shown to localize at the telomere and be associated with the Terminin complex. Sse is known to have a major role in the initiation of anaphase in cell division, but has only recently been shown to be involved in the Terminin complex, and its specific role is still being determined. Except for verrochio, which has a bioinformatically derived predicted structure, there is no data showing the physical structure of any of the subunits of this complex, representing a lack of information related to how the individual proteins play a role in the larger Terminin complex. Here, we present a well-established protocol for the expression and purification of some of these proteins, as well as their crystallization screenings. From these crystal-screening assays and follow-up experiments, the physical structure of the Terminin complex proteins can be elucidated. These results can bring to light its previously unknown structures, and how these proteins interact through their interactive domains.  <br/>

Progression towards structural determination and the understanding of protein-protein interactions of terminin complex proteins

255th National Meeting (2018)

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