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Majee"],"technology_type":["Mass Spectrometry","Gel-based experiment"],"software":["Not available"],"submitter_keywords":["Sheath blight disease","Osaldh","Ospbz1.","Isoasp","Pimt","Protein repair","Rhizoctonia solani","Ros homeostasis","Rice"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD080366"],"tissue":["Leaf"],"sample_protocol":["1. Sample- Total proteins extracted from infected rice sheath tissue immunoprecipitated with an anti-PIMT antibody. Bound proteins were eluted directly into SDS loading dye, which facilitated their subsequent separation on a 12% SDS-PAGE gel. Following electrophoresis, protein bands were carefully excised from the gel. These excised gel pieces then underwent in-gel tryptic digestion. After tryptic digestion, the resultant peptides were vacuum-dried and then reconstituted in 0.1% formic acid, preparing them for downstream LC-MS/MS analysis.  2. Purified 50µg recombinant OsALDH, OsPBZ1 proteins were incubated with 30mM H₂O₂ at 25°C for 4h. Samples were subjected to 12% SDS-PAGE. Subsequently, in-gel trypsin digestion was carried out, followed by LC-MS/MS analysis to identify residues prone to isoAsp modifications. ESI mass spectra of tryptic peptides were acquired using protein pilot software.  3. Instrument: LC-MS/MS was performed on an AB Sciex 400 Triple TOF 6600 mass spectrometer, integrated with an Ekspert nano-LC."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw LC-MS/MS data were initially processed using Analyst 1.7 (AB Sciex). Subsequent peptide and protein identification was performed using the Paragon method implemented in Protein Pilot v5.0.1. Peak lists generated were searched against the UniProt Oryza sativa proteome database, encompassing 453,874 protein entries. The database interrogation in Protein Pilot employed standard tryptic peptides, permitting up to three missed cleavages. Identifications were validated with a 1% false discovery rate (FDR). Mass tolerances were configured at 0.7Da for-precursor ions and 0.6Da for-fragment ions, respectively. Individual spectra were deemed acceptable for identification based on a confidence threshold of 95% and an unused score exceeding 1.3."],"omics_type":["Proteomics"],"labhead":["Dr Manoj Majee"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["BRIC-National Institute of Plant Genome Research, Aruna Asaf Ali Marg, New Delhi-110067"],"species":["Oryza Sativa (rice)"],"publication":["42481481 Gautam S, Kamble NU, Achary RK, Chandan RK, Varshney V, Hazra A, Laha S, Mahawar S, Mehandiratta S, Singh S, Jha G, Majee M. Rice PROTEIN L-ISOASPARTYL METHYLTRANSFERASES provides tolerance against sheath blight disease and repairs ALDH and PBZ1. Nat Commun. 2026 17(1):8901 10.1038/s41467-026-75618-0"],"submitter_mail":["manojmajee@nipgr.ac.in"],"submitter_affiliation":["National Institute of Plant Genome Research, New Delhi"],"submitter_country":["India"],"pubmed_abstract":["Protein L-isoaspartyl methyltransferase (PIMT) regulates key seed traits and abiotic stress tolerance in plants by repairing isoaspartyl (isoAsp) damaged proteins. However, whether PIMT-mediated repair is induced and is required during biotic stress tolerance remains unknown. Using rice lines with OsPIMT overexpression, RNAi-mediated suppression, and genome editing, we show that PIMT enhances tolerance to sheath blight (ShB) caused by Rhizoctonia solani. OsPIMT restricts fungal penetration and colonization of rice sheaths. Co-immunoprecipitation coupled with LC-MS/MS identify various proteins including antioxidant proteins, aldehyde dehydrogenases (ALDH) and pathogenesis-related protein 10 (PBZ1), that undergo isoAsp modification during R. solani infection and interact with PIMT. We show that OsALDH and OsPBZ1 exhibit intrinsic antifungal activity against R. solani, but isoAsp modification impairs their activity, making PIMT mediated repair important. Further, OsALDH enhances tolerance to R. solani by inhibiting lipid peroxidation and ROS homeostasis in rice and fungus. Overall, our study reveals that PIMT enhances ShB tolerance through the repair of isoAsp-damaged proteins important for disease tolerance."],"pubmed_title":["Rice PROTEIN L-ISOASPARTYL METHYLTRANSFERASES provides tolerance against sheath blight disease and repairs ALDH and PBZ1."],"pubmed_authors":["Gautam Shikha S, Kamble Nitin Uttam NU, Achary Rakesh Kumar RK, Chandan Ravindra Kumar RK, Varshney Vishal V, Hazra Abhijit A, Laha Saroj S, Mahawar Shivangi S, Mehandiratta Sohela S, Singh Sarvanand S, Jha Gopaljee G, Majee Manoj M"],"additional_accession":[]},"is_claimable":false,"name":"Investigation of interacting proteins of PROTEIN L-ISOASPARTYL METHYLTRANSFERASE (PIMT) during ShB pathogenesis and identification of isoAsp accumulation in ALDH and PBZ1.","description":"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.","dates":{"publication":"2026-09-14","submission":"2026-06-30"},"accession":"PXD080366","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:57577","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:67352","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:1584","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:29064","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:273791","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:33554","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:171719","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:980415","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:66440","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:34878","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:237610","NEWT:95486","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:207340","NEWT:172271","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:595495","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:7375","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT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