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N ‐Linked glycosylation of Drosophila rhodopsin occurs exclusively in the amino‐terminal domain and functions in rhodopsin maturation
Author(s) -
Katanosaka Kimiaki,
Tokunaga Fumio,
Kawamura Satoru,
Ozaki Koichi
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00160-4
Subject(s) - rhodopsin , glycosylation , biochemistry , biology , extracellular , microbiology and biotechnology , chemistry , retinal
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.