Functional coupling of presequence processing and degradation in human mitochondria

Kücükköse, C., Taskin, A.A., Marada, A., Brummer, T., Dennerlein, S. and Vögtle, F.‐N. (2020), FEBS J. doi:10.1111/febs.15358

The mitochondrial proteome is built and maintained mainly by import of nuclear‐encoded precursor proteins. Most of these precursors use N‐terminal presequences as targeting signals that are removed by mitochondrial matrix proteases. The essential mitochondrial processing protease MPP cleaves presequences after import into the organelle thereby enabling protein folding and functionality. The cleaved presequences are subsequently degraded by peptidases. While most of these processes have been discovered in yeast, characterization of the human enzymes is still scarce.