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John Rakus

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Mammalian C-linked glycosylation.


Approximately 50% of all human proteins are post-translationally modified by way of addition of a carbohydrate. Nearly all of these glycosylation reactions involve attachment of the carbohydrate molecule to either nitrogen on asparagine amino acids (N-linked) or oxygen on either serine or threonine amino acids (O-linked). However, a small group of C-linked carbohydrates have been identified in which the sugar mannose is attached to tryptophan amino acids through a carbon-carbon bond at C2.

General Interests.

1. How is this bond formed? The C. elegans C-mannosyltransferase has recently been identifed as DPY-19. I am interested in studying the four mammalian homologues of DPY-19 to evaluate substrate specifity and catalysis. What amino acids are involved in this reaction? What is the chemical mechanism for action?

2. What proteins receive this modification? As of 2013, roughly one hundred or so proteins have been identified with at least one C-mannosyltryptophan. Based on sequence analysis, it is approximated that over 2500 human proteins may be C-mannosylated. I want to identify what proteins have this modification, and under what cirumstances.

3. Why do they receive this modification? I am interested in evaluating signaling mechanisms and protein-protein interactions to gain insight as to why this unusual glycosylation event is made.



Bacterial Biofilm Formation.





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