Regulation of the early genes in the N-linked glycosylation pathway
Date
1990
DOI
Authors
Barboza, Eliane dos Santos Porto
Henry M Goldman School of Graduate Dentistry (Boston University)
Version
OA Version
Citation
Abstract
Protein glycosylation at the asparagine residues (Nglycosylation)
is obligatory for eukaryotic cell function.
The early genes in the N-glycosylation pathway encode
glycosyltransferases that catalyze the synthesis of the
precursor oligosaccharide. To elucidate how this synthesis
is regulated three early genes, ALG7, ALGl and ALG2, of the
N-linked glycosylation pathway were analyzed in the yeast§..:..
cerevisiae. Transcripts of these genes were examined in
yeast cells grown under different nutritional conditions to
exponential and stationary phases. The results indicate
that, in the exponential phase, cells grown in minimal media
under glucose deprivation have the highest steady-state
levels for all the three gene transcripts, while in
stationary phase, the highest steady-state levels were
observed when cells were grown under optimal conditions.
Also, the steady-state transcript levels of ALG7, ALGl and
ALG2 are, at least, an order of magnitude higher in the
exponentially growing cells as compared to the stationary.
The differences are most obvious for the ALG7 gene. We have
also investigated the involvement of the ALG7 gene in the
physiology of the hamster parotid gland. [TRUNCATED]
Description
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Thesis (M.Sc.D.)--Boston University, Henry M. Goldman School of Graduate Dentistry, 1990 (Periodontology).
Includes bibliographical references: (leaves 52-55).
Thesis (M.Sc.D.)--Boston University, Henry M. Goldman School of Graduate Dentistry, 1990 (Periodontology).
Includes bibliographical references: (leaves 52-55).
License
This work is protected by copyright. Downloading is restricted to the BU community. If you are the author of this work and would like to make it publicly available, please contact open-help@bu.edu.