Positively charged amino acids at the N terminus of select mitochondrial proteins mediate early recognition by import proteins αβ'-NAC and Sam37.

ABSTRACT: A major challenge in eukaryotic cells is the proper distribution of nuclear-encoded proteins to the correct organelles. For a subset of mitochondrial proteins, a signal sequence at the N terminus (matrix-targeting sequence [MTS]) is recognized by protein complexes to ensure their proper translocation into the organelle. However, the early steps of mitochondrial protein targeting remain undeciphered. The cytosolic chaperone nascent polypeptide-associated complex (NAC), which in yeast is represented as the two different heterodimers αβ-NAC and αβ'-NAC, has been proposed to be involved during the early steps of mitochondrial protein targeting. We have previously described that the mitochondrial outer membrane protein Sam37 interacts with αβ'-NAC and together promote the import of specific mit

SUBMITTER: Avendano-Monsalve MC 

PROVIDER: S-EPMC9136113 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature