Identification of a novel MIPEP splice variant with altered substrate-binding properties.

ABSTRACT: Mitochondrial intermediate peptidase (MIPEP) is a mitochondrial signal peptidase that removes N-terminal amino acids from mitochondrial matrix proteins. We have identified a novel Mipep splice variant that lacks exons 15 and 16, which we termed "ΔMIPEP". We characterized the molecular features of ΔMIPEP by investigating its expression level in numerous mouse tissues and by performing a computer simulation that allows the prediction of protein structures and substrate-binding properties. ΔMipep mRNA was detected in all mouse tissues examined but at much lower levels than full-length Mipep. Structure prediction and docking simulation of full-length MIPEP and ΔMIPEP with substrates of MIPEP, such as malate dehydrogenase 2 (MDH2) and cytochrome c oxidase subunit 4,

SUBMITTER: Otani Y 

PROVIDER: S-EPMC12605189 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature