Fruit flies, such as <i>Drosophila melanogaster, </i>protect the ends of their telomeres through the use of the terminin complex. Similar to shelterin, the terminin complex functions as a type of cap that acts as a physical barrier between telomeres. Without this barrier, the host organism will view unprotected telomeres as double stranded breaks and attempt to repair them by the use of neighboring telomeres. The fusion of telomeres leads to asymmetrical breaks in bound chromosomes and leads to their destruction, thus causing failure in DNA replication. The terminin complex is composed of heterochromatin protein 1 (HP1), HP1-ORC Associating Protein (HOAP), Modigliani (Moi), Verrochio (Ver) and several other important proteins. Out these proteins, Moi serves as a stabilizer for that of HOAP, commonly viewed as the anchor protein for the other subunits, and prevents degradation of the complex. Presently, there is no data addressing the physical structure of the protein, thus representing a large well of information waiting to be uncovered. Here we present data detailing a protocol for the prime expression and isolation of Moi, and its subsequent crystal screening.<br/>

Progress towards the structural determination of the telomere associating protein Modigliani

255th National Meeting (2018)

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