Essential Glycosyltransferases in Schizosaccharomyces Pombe

Colussi, Paul Attilio

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Description

Title

Essential Glycosyltransferases in Schizosaccharomyces Pombe

Author(s)

Colussi, Paul Attilio

Issue Date

1997

Doctoral Committee Chair(s)

Peter A.B.Orlean

Department of Study

Biochemistry

Discipline

Biochemistry

Degree Granting Institution

University of Illinois at Urbana-Champaign

Degree Name

Ph.D.

Degree Level

Dissertation

Keyword(s)

Biology, Microbiology

Language

eng

Abstract

I cloned cDNAs encoding S. pombe, human and Caenorhabditis briggsiae Dol-P-Man synthases, all three of which lack a characteristic carboxy-terminal transmembrane region found on previously isolated Dol-P-Man synthases. Known Dol-P-Man synthases can therefore be divided into a 'human' or 'S. cerevisiae' class, although the two are functionally equivalent for I showed that the S. cerevisiae DPM1 gene and its human counterpart both complement the lethal dpm1$\sp+$ null mutation in S. pombe. The 'human' class of Dol-P-Man synthases, however, do not complement an S. cerevisiae dpm1 null mutant, and, unlike the S. cerevisiae class of enzymes, do not confer Dol-P-Man synthetic activity on E. coli cells. I propose that the 'human' class of Dol-P-Man synthase requires one or more auxiliary proteins for catalytic activity or to mediate membrane association. The facts that Dol-P-Man synthase is an essential enzyme in yeast, and that the Ustilago and Trypanosoma synthases are in a different class from the human enzyme, raises the possibility that Dol-P-Man synthase could be exploited as a target for selective inhibitors of pathogenic eukaryotic microbes.

Graduation Semester

1997

Type of Resource

text

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