Mechanism of Peptide Binding and Cleavage by the Human Mitochondrial Peptidase Neurolysin.

Teixeira PF, Masuyer G, Pinho CM, Branca RMM, Kmiec B, Wallin C, Wärmländer SKTS, Berntsson RP, Ankarcrona M, Gräslund A, Lehtiö J, Stenmark P, Glaser E

J. Mol. Biol. 430 (3) 348-362 [2018-02-02; online 2017-11-26]

Proteolysis plays an important role in mitochondrial biogenesis, from the processing of newly imported precursor proteins to the degradation of mitochondrial targeting peptides. Disruption of peptide degradation activity in yeast, plant and mammalian mitochondria is known to have deleterious consequences for organism physiology, highlighting the important role of mitochondrial peptidases. In the present work, we show that the human mitochondrial peptidase neurolysin (hNLN) can degrade mitochondrial presequence peptides as well as other fragments up to 19 amino acids long. The crystal structure of hNLN

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PubMed 29183787

DOI 10.1016/j.jmb.2017.11.011

Crossref 10.1016/j.jmb.2017.11.011

S0022-2836(17)30561-2