Synthesis and assembly of membrane glycoproteins: presence of leader peptide in nonglycosylated precursor of membrane glycoprotein of vesicular stomatitis virus.
- 1 February 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (2), 570-574
- https://doi.org/10.1073/pnas.76.2.570
Abstract
Translation of mRNA encoding vesicular stomatitis virus envelope glycoprotein G by a membrane-free ribosomal extract obtained from [human cervical carcinoma] HeLa cells yielded a nonglycosylated protein G1 (MW 63,000). In the presence of added microsomal membranes, G1 was converted to the glycosylated protein G2 (MW 67,000) which is inserted in the membrane vesicles as a transmembrane protein. Labeling with methionine donated by wheat germ initiator .**GRAPHIC**. showed that G1 but not G2 contains methionine in the NH2-terminal position. Determination of the NH2-terminal sequence of G1, G2 and G showed that a leader peptide of 16 amino acids is present in G1 but absent from the glycosylated proteins G2 and G. This leader peptide contains at least 62% hydrophobic amino acids and is removed presumably during insertion of G1 into the membrane.This publication has 33 references indexed in Scilit:
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