Today is Day 3 of the Experimental Biology 2015 conference here in Boston, MA, and it is getting good!
I woke up early today to head to a Post Translational Modifications Session on Arginine Modifications, and it was great! I learned a lot about the research that is going on in my field, and I got to meet another professor who I have collaborated with/tested some enzyme activity. The session was 2.5 hours long, but it seemed to fly by. Each talk was about 20ish minutes I believe, and there are some really interesting things going on in the arginine modification world! One of the most interesting things I learned is about Arginine Phosphorylation in bacteria! If you are knowledgable about the eukaryotic proteasome degradation system, you know that proteins get marked for degradation by ubiquitination, which then signals shuttling/entrance into the proteasome and then the protein will get degraded.
Apparently, some bacteria, specifically Bacillus subtilis have an arginine kinase, that originally was identified as a tyrosine kinase. First off, I didn't know that arginine could get phosphorylated. Second, this phosphorylation is thought to work as a degradation marker for the proteasome in these bacteria! I did not know about this. The fact that arginine, which is positively charged, can become a bulky entity with now a large negative charge, I guess it just never crossed my mind!
After this session, I attended a bioinformatics session on how to find proteins with unknown function through online database searches and groupings. I learned how to use new online tools that I will check out to learn more about my enzyme and its orthologs!
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