William J. Lennarz, Ph.D.
Department of Biochemistry and Cell Biology
Cell and Developmental Biology
Life Sciences Building
Stony Brook University
Stony Brook, NY 11794-5215
Office telephone: 631-632-8560
Biosynthesis and catabolism of glycoproteins
Our laboratory is interested in understanding several steps involved in glycoprotein
synthesis, including N-glycosylation and protein folding, as well as
the functions of the glycan chains. We are using yeast, a simple eukaryotic
organism that can be genetically manipulated, to study glycoprotein assembly.
More specifically, we are investigating the enzymatic processes of oligosaccharide
addition and removal that occur in nascent polypeptides and misfolded
glycoproteins, respectively ( fig.1 ). Evidence has been
obtained that the enzyme PNGase associates with the proteasome during
proteolysis of glycoproteins. In addition, PDI, the enzyme that catalyzes
folding and disulfide bond formation in glycoproteins, is being studied
( fig.2 ).
The crystal structure has been obtained and now we are studying the
role of the various domains of this protein in its catalytic activity.
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