A proline residue near the amino terminus of the mature domain of secretory proteins lowers the level of the proton motive force required for translocation-Reference-Cited by-同舟云学术

A proline residue near the amino terminus of the mature domain of secretory proteins lowers the level of the proton motive force required for translocation

Published:1991-05 Issue:15 Volume:266 Page:9977-9982
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Lu H.M.,Yamada H.,Mizushima S.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference36 articles.

1. In vitro translocation of bacterial secretory proteins and energy requirements

2. Efficient in vitro translocation into Escherichia coli membrane vesicles of a protein carrying an uncleavable signal peptide. Characterization of the translocation process.

3. SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.

4. The proton motive force lowers the level of ATP required for the in vitro translocation of a secretory protein in Escherichia coli.

5. A high Concentration of SecA Allows Proton Motive Force-independent Translocation of a Model Secretory Protein into Escherichia coli Membrane Vesicles

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