A snapshot of the Physcomitrella N-terminome reveals N-terminal methylation of organellar proteins.

ABSTRACT:

Key message

Analysis of the N-terminome of Physcomitrella reveals N-terminal monomethylation of nuclear-encoded, mitochondria-localized proteins. Post- or co-translational N-terminal modifications of proteins influence their half-life as well as mediating protein sorting to organelles via cleavable N-terminal sequences that are recognized by the respective translocation machinery. Here, we provide an overview on the current modification state of the N-termini of over 4500 proteins from the model moss Physcomitrella (Physcomitrium patens) using a compilation of 24 N-terminomics datasets. Our data reveal distinct proteoforms and modification states and confirm predicted targeting peptide cleavage sites of 1,144 proteins localized to plastids and the thylakoid lumen, to mitochondria,

SUBMITTER: Hoernstein SNW 

PROVIDER: S-EPMC11450134 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature