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Secretory protein synthesis in Chironomus salivary gland cells is not coupled with protein translocation across endoplasmic reticulum membranes
Author(s) -
Kiseleva E.V.
Publication year - 1989
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 - 10.1016/0014-5793(89)81545-5
Subject(s) - endoplasmic reticulum , polysome , secretory protein , sec61 , membrane , microbiology and biotechnology , salivary gland , secretory pathway , stim1 , secretion , protein biosynthesis , biology , chemistry , biochemistry , ribosome , membrane protein , golgi apparatus , translocon , rna , gene
Fragments of rough endoplasmic reticulum containing polysomes bound to the membranes only at the 5' end were visualized in electron microscopic spreads from Chironomus thummi salivary gland cells. The length of the nascent protein molecules in the polysemes increased from the 5' to the 3' (free) polysome end. The data obtained disagree with the generally accepted model according to which synthesis of secretory proteins is concomitant with the protein transport across the endoplasmic membrane