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Requirement of N-linked glycosylation site in Drosophila rhodopsin.

作者信息

O'Tousa J E

机构信息

Department of Biological Sciences, University of Notre Dame, IN 46556.

出版信息

Vis Neurosci. 1992 May;8(5):385-90. doi: 10.1017/s0952523800004910.

DOI:10.1017/s0952523800004910
PMID:1534022
Abstract

In vitro mutagenesis and germline transformation were used to create a Drosophila mutant, delta Asn20, lacking the N-linked glycosylation site near the amino terminus of the major rhodopsin (Asn20-Gly-Ser changed to Ile-Gly-Ser). Low opsin protein levels are detected in delta Asn20 photoreceptors. Electroretinogram responses of mutant flies show that the residual rhodopsin found in this mutant is capable of initiating phototransduction. The organization of rhabdomeres, the photoreceptor organelle containing nearly all of the rhodopsin, is aberrant in the delta Asn20 mutant and undergoes age-dependent deterioration. These results establish that an N-linked glycosylation site, and likely glycosylation itself, plays a critical role in the maturation of Drosophila rhodopsin.

摘要

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