‘With the help of a Biochemical Society General Travel Grant I attended the Eighth International Fission Yeast Meeting in the beautiful Ikuta Shrine in downtown Kobe, Japan, from June 21-26 2015.
The meeting began with a series of special lectures from four of the leading figures in the fission yeast world – Mitsuhiro Yanagida (Okinawa Institute of Science and Technology, Japan), Paul Russell (Scripps Research Institute, USA), Masayuki Yamamoto (National Institute of Basic Biology, Japan) and Paul Nurse (Crick Institute, UK) – and set the standard for a week of excellent science covering topics as diverse as epigenetics and chromatin, DNA replication, repair and recombination, cell morphology and cell polarity, mitosis, meiosis and cytokinesis. Across around 100 talks and 150 posters, the quality of the science on show was excellent: understanding the biology of fission yeast was the common theme, of course, with traditional genetic and biochemical approaches increasingly being bolstered by state-of-the-art omics methodologies.
Thanks to the support from the Biochemical Society I was able to present a poster describing work done in my lab at the University of St Andrews by two very talented undergraduate students, Sarah Musto and Emma Cottell, both now graduated, describing the application of a proximity labeling technique to study protein-protein interactions (PPI’s) within the fission yeast DNA replication apparatus.
The technique (named ID-PRIME for Interaction-Dependent Probe Incorporation by Enzymes by its developers, Alice Ting and colleagues at MIT) relies on the ability of the bacterial lipoic acid ligase enzyme LplA to lipoylate a short acceptor peptide LAP1. We’ve created reagents to allow LplA and LAP1 tagging of proteins expressed at normal endogenous levels in fission yeast and demonstrated LplA- and lipoic acid-dependent lipoylation of interacting LAP1-tagged protein partners.
Excitingly, the technique offers the possibility of detecting transient protein-protein interactions through short lipoic acid labeling times and thus should prove to be a valuable tool for studying PPI’s that exhibit dynamic behaviour through the cell cycle. A manuscript describing our work is now in preparation but already I have already sent out reagents to several colleagues who took time to visit the poster and who are keen to apply the technique to their particular proteins of interest.’