N-tail translocation of mature beta-lactamase across the Escherichia coli cytoplasmic membrane

FEBS Letters
C MitsopoulosJ K Broome-Smith

Abstract

Mature beta-lactamase was attached to the N-terminus of human glycophorin C, an N-out membrane protein lacking a cleavable signal peptide (an N-tail membrane protein). When synthesised in Escherichia coli more than 30% of the intact mature beta-lactamase-glycophorin C molecules assembled N-out, C-in into the cytoplasmic membrane. The N-tail translocated beta-lactamase folded into an enzymatically active form, but it was more susceptible to proteolysis than the equivalent portion of beta-lactamase-glycophorin C synthesised with an N-terminal signal peptide. Its translocation was virtually abolished when the N-out domain of glycophorin C was truncated or when the basic residues C-terminally flanking the glycophorin C membrane-spanning segment were replaced with neutral ones.

References

Dec 1, 1990·Protein Engineering·G von Heijne, C Manoil
Oct 1, 1990·Molecular Microbiology·J K Broome-SmithY Zhang
Jan 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·T A Kunkel
Oct 1, 1995·Trends in Cell Biology·R E DalbeyG von Heijne

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Citations

Jan 15, 2019·Journal of Molecular Biology·Sri Karthika ShanmugamRoss E Dalbey

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