KERSCHER, S and ALBERT, S and WUCHERPFENNIG, D and HEISENBERG, M and SCHNEUWLY, S (1995) MOLECULAR AND GENETIC-ANALYSIS OF THE DROSOPHILA MAS-1 (MANNOSIDASE-1) GENE WHICH ENCODES A GLYCOPROTEIN PROCESSING ALPHA-1,2-MANNOSIDASE. DEVELOPMENTAL BIOLOGY, 168 (2). pp. 613-626. ISSN 0012-1606, 1095-564X
Full text not available from this repository.Abstract
Glycosylation is an important mechanism for modulating the physicochemical and biological properties of proteins in a stage- and tissue-specific manner. The enzymology of this process is just beginning to be understood. Here we present the molecular analysis of mas-1 (mannosidase-1), a Drosophila gene with significant homologies to mammalian and Saccharomyces cerevisiae glycoprotein processing alpha 1,2-mannosidases. An enhancer-trap P-element inserted upstream of nas-1 leads to highly specific lacZ expression in the lobula plate giant neurons, cells that mediate the large-field optomotor response. This staining, however, seems to reflect only a small part of the complex expression pattern of the mas-1 gene: Two promoters produce alternative transcripts that show individual spatial distributions during embryonic development, including a maternal contribution. Both transcripts code for type II transmembrane proteins which differ in their N-terminal parts. Null mutants in mas-1 display defects in the embryonic PNS, in the wing, and in the adult eye. These findings illustrate that the processing of N-linked glycans plays a functional role in Drosophila development, There is, however, ample evidence for genetic and biochemical redundancy in the mannose-trimming steps of this pathway. (C) 1995 Academic Press, Inc.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MEDIATED ENHANCER DETECTION; ALPHA-MANNOSIDASE; SACCHAROMYCES-CEREVISIAE; HORSERADISH-PEROXIDASE; PROTEIN GLYCOSYLATION; CARBOHYDRATE EPITOPE; GRASSHOPPER EMBRYOS; CELL-SURFACE; MELANOGASTER; SEQUENCE; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:37 |
| URI: | https://pred.uni-regensburg.de/id/eprint/52619 |
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