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Enhanced synthesis of the glucose/calcium‐regulated proteins in a hamster cell mutant deficient in transfer of oligosaccharide core to polypeptides
Author(s) -
Lee Amy S.,
Wells Steven,
Kim Kyu Seong,
Scheffler Immo E.
Publication year - 1986
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041290302
Subject(s) - mutant , complementation , chinese hamster ovary cell , glycosylation , chinese hamster , mutation , gene , biology , transcription (linguistics) , biochemistry , calcium , microbiology and biotechnology , chemistry , cell culture , dna , genetics , linguistics , philosophy , organic chemistry
The properties of two Chinese hamster temperature‐sensitive mutants, K12 and H3.5, were examined. Both mutants originated from the same parental cell line, Wg1A, and were isolated as cell cycle mutants arrested in G1. Previously, we had been shown that the H3.5 ts mutation affected the transfer of the oligosaccharide from the lipid carrier to the nascent polypeptide and that the K12 ts mutation regulated the transcription of two glucose/calcium‐regulated genes. We report here that these two mutants exhibit almost identical phenotypes at the biochemical level. Furthermore, a genetic complementation test demonstrates that the two ts lesions must be closely related, or even identical. Our results suggest that a specific defect in glycosylation may result in the overproduction of the glucose/calcium‐regulated proteins and is capable of activating the promoter of the major glucose‐regulated gene.