02751nas a2200277   4500008004100000022001400041245012500055210006900180260006400249300001200313490000800325520173500333653000902068653003702077653003202114653000902146653001302155653002102168653003002189653004702219100002002266700002002286700002002306700001702326856013002343       2009                        eng d  a0027-551400aIdentification of Indian pathogenic races of fusarium oxysporum f. sp ciceris with gene specific, ITS and random markers0 aIdentification of Indian pathogenic races of fusarium oxysporum   a810 E 10TH ST, LAWRENCE, KS 66044 USAbALLEN PRESS INCcAUG  a484-4950 v1013 a<p>In this study we demonstrate the synergistic use of gene-specific markers, ITS-RFLP, ISSR and AFLP for distinguishing Indian F. oxysporum f. sp. ciceris races. We also report for the first time that F. oxysporum f. sp. ciceris race 3, a wilt pathogen of chickpea in India, is actually E proliferatum based on phylogenetic analysis with EF-1 alpha sequence data. E oxysporum f. sp. ciceris races 1, 2 and 4 were easily distinguished from ``race 3'' (F. proliferatum) by PCR amplification with oligonucleotides designed from conserved regions of Hop78 transposon (Hop 78), cutinase (Cut), desaturase (Dst). F oxysporum f. sp. ciceris race 4 was distinguished with the xylanase 3 (xyl3) gene by absence of amplification product only in this race. The Xyl3 amplified-DNA fragment isolated and sequenced from E oxysporum f. sp. ciceris race I was similar to the F-xylanase (Xyl3) gene of E oxysporum f. sp. lycopersici. A TELD motif, which is characteristic of the F-xylanases family, was detected within the deduced amino acid sequence of F. oxysporum f. sp. ciceris. Similarly the F oxysporum f. sp. ciceris Hop78 DNA fragment, which identified ``race 3'' (E proliferatum), was homologous to the Hop78 transposon of E oxysporum f. sp. melonis, including the 100 amino acid conserved domain and the characteristic CCHC motif. The internal transcribed spacer region-restriction fragment length polymorphism (ITS-RFLP) approach along with intersimple sequence repeat (ISSR) method also differentiated ``race 3'' (F. proliferatum). Races 1 and 2 were identified by unique AFLP patterns. Sequence characterization of race-specific AFLP products revealed significant homologies of these sequences with metabolically important genes.</p>10aAFLP10aF. oxysporum f. sp ciceris races10agene specific amplification10aISSR10aITS-RFLP10arace delineation10asequence characterization10atranslation elongation factor (EF-1 alpha)1 aGurjar, Gayatri1 aBarve, Maneesha1 aGiri, Ashok, P.1 aGupta, Vidya  uhttps://library.ncl.res.in/content/identification-indian-pathogenic-races-fusarium-oxysporum-f-sp-ciceris-gene-specific-its-001870nas a2200181   4500008004100000245010100041210006900142260000800211300001400219490000700233520122200240100002201462700001901484700002001503700002001523700001701543856012801560       2017                        eng d00aIdentification and functionality prediction of pathogenesis-related protein 1 from legume family0 aIdentification and functionality prediction of pathogenesisrelat  cNOV  a2066-20800 v853 aThe production and accumulation of pathogenesis-related (PR) proteins in plants is one of the important responses to biotic and abiotic stress. Large number of identified PR proteins has been categorized into 17 functional families based on their structure, phylogenetics, and biological activities. However, they are not widely studied in legume crops. Using 29 PR1 proteins from Arabidopsis thaliana, as query, here we have predicted 92 candidate PR1 proteins through the PSI-BLAST and HMMER programs. These candidate proteins were comprehensively analyzed with, multiple sequence alignment, domain architecture studies, signal peptide, and motif extraction followed by phylogenetic analysis. Further, response of two candidate PR1 proteins from chickpea against Fusarium oxysporum f.sp.ciceri attack was validated using qRT-PCR followed by their 3D structure prediction. To decipher mode of action for PR1s, docking of pathogen extracellular matrix components along with fungal elicitors was performed with two chickpea PR1 proteins. Based on these findings, we propose carbohydrate to be the unique pathogen-recognition feature for PR1 proteins and beta-glucanase activity via beta-glucan binding or modification.1 aTellis, Meenakshi1 aMathur, Monika1 aGurjar, Gayatri1 aKadoo, Narendra1 aGupta, Vidya  uhttps://library.ncl.res.in/content/identification-and-functionality-prediction-pathogenesis-related-protein-1-legume-family