Monday, January 18, 2016
O-man glycosylations in yeast
It might be time to consider changing the name of one prestigious journal to MCgP, cause the glycoproteomics just keeps coming!
This solid new paper from Patrick Neubert et. al., goes out and explores O-mannose glycosylation in yeast. Yeast? I know what you're thinking....
Wait a second, though! It turns out that yeast is the ideal model here. Cause this O-man glycosylation is the only O glycosylation that yeast get and we don't have a great feel for optimizing parameters for studying it. By building the methods and showing that it works in yeast we can take this method over and study these important glycosylation events in organisms that aren't yeast.
To get deep coverage, proteins were digested with three different enzymes (LysC, LysN, AspN) and a combination of HCD/ETD was optimized for each digest using an Orbitrap Velos and Fusion.
They weren't satisfied with building a methodology here, either. They look deeply into the structures of the glycopeptides they study and even look at 3-dimensional interactions that suggest the presence of some glycosylations have a negative effect on the formation of others in the same 3D space. So, not only do you have a new methodology for studying an important glycosylation family, but you also have some sweet new basic science uncovered. Turns out we still don't know everything there is to know about even model organisms like baker's yeast!