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.
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CITATION STYLE
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
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