Dual functions of the signal peptide in protein transfer across the membrane

Jack Coleman, Masatoshi Inukai, Masayori Inouye

Research output: Contribution to journalArticlepeer-review

48 Scopus citations

Abstract

Most secretory proteins in both prokaryotic and eukaryotic cells are synthesized from a precursor with an amino-terminal extension of 20 to 25 amino acid residues called a signal peptide. These signal peptides are removed during translocation of the secretory proteins across the membrane. When two precursor structures are fused, the internalized second signal peptide was found to exert two different roles, depending upon either the distance between the two signal peptides, or whether the first signal peptide functions cotranslationally or posttranslationally. One role is to function as the usual signal peptide to translocate the protein downstream of the internal signal peptide. The other role is to function as a stop-transfer signal to create a transmembrane protein with the second signal peptide anchoring the protein in the membrane.

Original languageEnglish (US)
Pages (from-to)351-360
Number of pages10
JournalCell
Volume43
Issue number1
DOIs
StatePublished - Nov 1985
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

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