Proteome-wide identification of methylglyoxalated proteins in rapeseed (Brassica napus L.).
Plant Physiol Biochem
; 207: 108319, 2024 Feb.
Article
de En
| MEDLINE
| ID: mdl-38183900
ABSTRACT
Methylglyoxal (MG), a highly reactive cellular metabolite, is crucial for plant growth and environmental responses. MG may function by modifying its target proteins, but little is known about MG-modified proteins in plants. Here, MG-modified proteins were pulled down by an antibody against methylglyoxalated proteins and detected using liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis. We identified 543 candidate proteins which are involved in multiple enzymatic activities and metabolic processes. A great number of candidate proteins were predicted to localize to cytoplasm, chloroplast, and nucleus, consistent with the known subcellular compartmentalization of MG. By further analyzing the raw LC-MS/MS data, we obtained 42 methylglyoxalated peptides in 35 proteins and identified 10 methylglyoxalated lysine residues in a myrosinase-binding protein (BnaC06G0061400ZS). In addition, we demonstrated that MG modifies the glycolate oxidase and ß-glucosidase to enhance and inhibit the enzymatic activity, respectively. Together, our study contributes to the investigation of the MG-modified proteins and their potential roles in rapeseed.
Mots clés
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Brassica napus
/
Brassica rapa
Type d'étude:
Diagnostic_studies
Langue:
En
Journal:
Plant Physiol Biochem
/
Plant, physiology and biochemistry
/
Plant. physiol. biochem
Sujet du journal:
BIOQUIMICA
/
BOTANICA
Année:
2024
Type de document:
Article
Pays d'affiliation:
Chine
Pays de publication:
France