Quantitative glycoproteomics identifies target N-glycoproteins of the Golgi-class I α-mannosidase SlMNSI1 that is important for tomato fruit development.

ABSTRACT: Protein N-glycosylation is a fundamental post-translational modification, yet its role in regulating fruit development remains poorly understood. Here, we investigated the function of the class I α-mannosidase SlMNSI1 in tomato (Solanum lycopersicum) using chemical genetics, CRISPR-Cas9-mediated gene editing, quantitative site-specific glycoproteomics, and genetic complementation analyses. Inhibition of SlMNSI by kifunensine or SlMNSI1 knockout caused severe pleiotropic defects and impaired fruit development, leading to the accumulation of Man₉GlcNAc₂ or Man₈GlcNAc₂, respectively, on glycoprotein substrates. Analysis of the tomato fruit site-specific N-glycoproteome identified 3091 intact N-glycopeptides containing 873 N-glycosites and 158 N-glyc

SUBMITTER: Zhao XY 

PROVIDER: S-EPMC12744743 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature