GLYCAN STRUCTURE & POSITION OF GLYCOSYLATION SITES ON DSIAT

$2,610P41FY2010RRNIH

University Of Georgia, Athens GA

Investigators

Linked publications & trials

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Abstract

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The Drosophila sialytransferase (DSiaT) gene, which is closely related to the vertebrate ST6Gal sialytransferase family, has been characterized recently and the in vitro enzymatic activity and acceptor specificity has been determined. As in vitro acceptors, this enzyme was found to prefer terminal LacdiNAc and LacNAc residues found on N-linked glycans of glycoproteins (Koles, et al., 2004). In this collaborative work, we are performing the analysis of glycan structure and the site(s) of glycosylations on the DSiaT. Our data show that the N-glycan structure of the DSiaT has a fucosylated high-mannose type (Man3GlcNAc2Fuc1) as the main component. We are currently working on the mapping of N-glycosylation sites.

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