skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Characterization of new mutants in the early part of the yeast secretory pathway isolated by a (/sup 3/H)mannose suicide selection

Abstract

We have adapted a (/sup 3/H)mannose suicide selection to identify mutations in additional genes which function in the early part of the yeast secretory pathway. Thus far this protocol has led to the identification of two new genes which are implicated in this process, as well as additional alleles of previously identified genes. The new mutants, bet1 and bet2, are temperature sensitive for growth and protein transport. Thin section analysis has revealed the accumulation of a network of endoplasmic reticulum (ER) at the restrictive temperature (37/sup 0/C). Precursors of exported proteins that accumulate in the cell at 37/sup 0/C are terminally core glycosylated. These observations suggest that the transport of precursors is blocked subsequent to translocation into the ER but before entry into the Golgi apparatus. The bet1 and bet2 mutants define two new complementation groups which have the same properties as previously identified ER-accumulating mutants. This and previous findings suggest that protein exit from the ER and entry into the Golgi apparatus is a complex process requiring at least 11 genes.

Authors:
;
Publication Date:
Research Org.:
Yale Univ. School of Medicine, New Haven, CT
OSTI Identifier:
5669997
Resource Type:
Journal Article
Journal Name:
J. Cell Biol.; (United States)
Additional Journal Information:
Journal Volume: 105:4
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; MUTANTS; CHEMICAL COMPOSITION; PROTEINS; MEMBRANE TRANSPORT; SECRETION; SACCHAROMYCES CEREVISIAE; GENE MUTATIONS; ACID PHOSPHATASE; BIOLOGICAL PATHWAYS; ENDOPLASMIC RETICULUM; GENES; MANNOSE; MOLECULAR WEIGHT; PEPTIDES; TRACER TECHNIQUES; TRITIUM COMPOUNDS; ALDEHYDES; CARBOHYDRATES; CELL CONSTITUENTS; ENZYMES; ESTERASES; FUNGI; HEXOSES; HYDROLASES; ISOTOPE APPLICATIONS; LABELLED COMPOUNDS; MICROORGANISMS; MONOSACCHARIDES; MUTATIONS; ORGANIC COMPOUNDS; ORGANOIDS; PHOSPHATASES; PLANTS; SACCHARIDES; SACCHAROMYCES; YEASTS; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Newman, A.P., and Ferro-Novick, S. Characterization of new mutants in the early part of the yeast secretory pathway isolated by a (/sup 3/H)mannose suicide selection. United States: N. p., 1987. Web. doi:10.1083/jcb.105.4.1587.
Newman, A.P., & Ferro-Novick, S. Characterization of new mutants in the early part of the yeast secretory pathway isolated by a (/sup 3/H)mannose suicide selection. United States. doi:10.1083/jcb.105.4.1587.
Newman, A.P., and Ferro-Novick, S. Thu . "Characterization of new mutants in the early part of the yeast secretory pathway isolated by a (/sup 3/H)mannose suicide selection". United States. doi:10.1083/jcb.105.4.1587.
@article{osti_5669997,
title = {Characterization of new mutants in the early part of the yeast secretory pathway isolated by a (/sup 3/H)mannose suicide selection},
author = {Newman, A.P. and Ferro-Novick, S.},
abstractNote = {We have adapted a (/sup 3/H)mannose suicide selection to identify mutations in additional genes which function in the early part of the yeast secretory pathway. Thus far this protocol has led to the identification of two new genes which are implicated in this process, as well as additional alleles of previously identified genes. The new mutants, bet1 and bet2, are temperature sensitive for growth and protein transport. Thin section analysis has revealed the accumulation of a network of endoplasmic reticulum (ER) at the restrictive temperature (37/sup 0/C). Precursors of exported proteins that accumulate in the cell at 37/sup 0/C are terminally core glycosylated. These observations suggest that the transport of precursors is blocked subsequent to translocation into the ER but before entry into the Golgi apparatus. The bet1 and bet2 mutants define two new complementation groups which have the same properties as previously identified ER-accumulating mutants. This and previous findings suggest that protein exit from the ER and entry into the Golgi apparatus is a complex process requiring at least 11 genes.},
doi = {10.1083/jcb.105.4.1587},
journal = {J. Cell Biol.; (United States)},
number = ,
volume = 105:4,
place = {United States},
year = {1987},
month = {10}
}