Ontology highlight
ABSTRACT:
SUBMITTER: Yim C
PROVIDER: S-EPMC8277137 | biostudies-literature | 2021 Jul
REPOSITORIES: biostudies-literature
Yim Chewon C Chung Yeonji Y Kim Jeesoo J Nilsson IngMarie I Kim Jong-Seo JS Kim Hyun H
Journal of cell science 20210709 13
Signal peptidase (SPase) cleaves the signal sequences (SSs) of secretory precursors. It contains an evolutionarily conserved membrane protein subunit, Spc1, that is dispensable for the catalytic activity of SPase and whose role remains unknown. In this study, we investigated the function of yeast Spc1. First, we set up an in vivo SPase cleavage assay using variants of the secretory protein carboxypeptidase Y (CPY) with SSs modified in the N-terminal and hydrophobic core regions. When comparing t ...[more]