Post-translation modifications (PTMs) are significantly critical for almost all proteins, especially in regulating many biological processes. My question: since one protein can possess multiple biological functions, do that protein always needs its PTMs version to perform all of these functions? In the other words, is it possible that the protein without PTMs version still works like its PTMs version in a certain process/function? Thank you.
Hi,
Interesting question!
I think the answer to your question is: yes, an unmodified protein can still fullfil some of its functions. Take an IgG1 for example: the unmodified, i.e. non-glycosylated, protein is capable of binding its antigen, due to the structural arrangement of its complementarity-determining regions, but due to the lack of glycosylation, it cannot induce any effector function, for which (certain types of) glycans are required.
The same goes, for example, for proteins that interact with histones via electrostatic interactions (e.g. through stretches of acidic amino acids), but that will only recruit secondary interaction partner proteins once it gets, for example, phosphorylated.
Hope this helps!
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