Functional mapping of N-terminal residues in the yeast proteome uncovers novel determinants for mitochondrial protein import.

ABSTRACT: N-terminal ends of polypeptides are critical for the selective co-translational recruitment of N-terminal modification enzymes. However, it is unknown whether specific N-terminal signatures differentially regulate protein fate according to their cellular functions. In this work, we developed an in-silico approach to detect functional preferences in cellular N-terminomes, and identified in S. cerevisiae more than 200 Gene Ontology terms with specific N-terminal signatures. In particular, we discovered that Mitochondrial Targeting Sequences (MTS) show a strong and specific over-representation at position 2 of hydrophobic residues known to define potential substrates of the N-terminal acetyltransferase NatC. We validated mitochondrial precursors as co-translational targets of NatC by selectiv

SUBMITTER: Nashed S 

PROVIDER: S-EPMC10482271 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature