N‐Linked glycosylation of Drosophila rhodopsin occurs exclusively in the amino‐terminal domain and functions in rhodopsin maturation

FEBS Letters

Ozaki, Koichi¹  Tokunaga, Fumio²  Kawamura, Satoru¹  Katanosaka, Kimiaki¹ 

[1] Department of Biology, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka,Osaka 560,Japan;Department of Earth and Space Science, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka,Osaka 560,Japan

关键词: Rhodopsin;    ninaE;    Glycosylation;    Photoreceptor cell;    Protein maturation;    Drosophila melanogaster;    ROS;    rod photoreceptor outer segment;    rER;    rough endoplasmic reticulum;    PCR;    polymerase chain reaction;    SDS;    sodium dodecyl sulfate;    PAGE;    polyacrylamide gel electrophoresis;    PNGaseF;    peptide-N-glycosidase F;    PPIase;    peptidylproline cis-trans-isomerase;   

DOI  :  10.1016/S0014-5793(98)00160-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown