Investigation of interacting proteins of PROTEIN L-ISOASPARTYL METHYLTRANSFERASE (PIMT) during ShB pathogenesis and identification of isoAsp accumulation in ALDH and PBZ1.

ABSTRACT: 1. The formation of isoAsp residues from Asp and Asn residues in proteins and peptides is accelerated under stressful environments and has detrimental effects on protein structure and function. PROTEIN L-ISOASPARTYL METHYLTRANSFERASE (PIMT) is a protein repairing enzyme which revert such deleterious isoAsp residues to normal aspartyl residues as a protein repair process. In present work, we identify the probable interactors of PIMT during pathogenesis in rice. Co-immunoprecipitation coupled with LC-MS/MS identified antioxidant proteins, including aldehyde dehydrogenases (ALDH) and pathogenesis-related protein 10 (PBZ1), as targets of isoAsp modification during R. solani infection. We show that OsALDH and OsPBZ1 exhibit intrinsic antifungal activity against R. solani, but isoAsp modification significantly impairs their activity, making PIMT mediated repair important. 2. To further investigated whether oxidative stress could directly induce such modifications in-vitro. purified recombinant OsALDH and OsPBZ1 proteins were exposed to 30mM H2O2 at 25°C. MS/MS analyses were carried out to identify isoAsp modifications. MS analyses suggest that these enzymes are susceptible to isoAsp formation under oxidative stress.

INSTRUMENT(S):

ORGANISM(S): Oryza Sativa (rice)

TISSUE(S): Leaf

SUBMITTER: Manoj Majee  

LAB HEAD: Dr Manoj Majee

PROVIDER: PXD080366 | Pride | 2026-09-14

REPOSITORIES: Pride