Dislocation by the m-AAA protease increases the threshold hydrophobicity for retention of transmembrane helices in the inner membrane of yeast mitochondria

14Citations
Citations of this article
32Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

Background: The m-AAA protease dislocates transmembrane segments from the mitochondrial inner membrane. Results: The presence of the m-AAA protease increases the hydrophobicity required for a transmembrane segment to remain in the membrane. Conclusion: The hydrophobicity thresholds for transmembrane segment retention in the mitochondrial inner membrane differ with or without the m-AAA protease. Significance: Retention of a transmembrane domain in the inner membrane depends on recognition by the m-AAA protease.© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

Cite

CITATION STYLE

APA

Botelho, S. C., Tatsuta, T., Von Heijne, G., & Kim, H. (2013). Dislocation by the m-AAA protease increases the threshold hydrophobicity for retention of transmembrane helices in the inner membrane of yeast mitochondria. Journal of Biological Chemistry, 288(7), 4792–4798. https://doi.org/10.1074/jbc.M112.430892

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free