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 Lettjournal_title
FEBS lettersauthors
Katanosaka K,Tokunaga F,Kawamura S,Ozaki Kdoi
10.1016/s0014-5793(98)00160-4subject
Has Abstractpub_date
1998-03-13 00:00:00pages
149-54issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(98)00160-4journal_volume
424pub_type
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