N-linked glycosylation of Drosophila rhodopsin occurs exclusively in the amino-terminal domain and functions in rhodopsin maturation.

Abstract:

:Immature Drosophila rhodopsin is N-glycosylated, but undergoes complete deglycosylation during the process of protein maturation. In order to elucidate the site of glycosylation and its role in rhodopsin synthesis, we investigated the in vitro and in vivo synthesis of rhodopsin whose putative N-glycosylation sites (Asn-20 and Asn-196) were replaced by isoleucine. The results demonstrated that immature rhodopsin binds a single oligosaccharide chain exclusively at Asn-20 in the N-terminal extracellular domain. Furthermore, the results gave the first evidence directly indicating that deletion of the oligosaccharide chain markedly impedes rhodopsin maturation.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Katanosaka K,Tokunaga F,Kawamura S,Ozaki K

doi

10.1016/s0014-5793(98)00160-4

subject

Has Abstract

pub_date

1998-03-13 00:00:00

pages

149-54

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)00160-4

journal_volume

424

pub_type

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