02856nas a2200277 4500008004100000022001400041245009000055210006900145260005700214300001200271490000800283520193300291653001002224653001302234653002202247653001302269653002502282100002202307700002002329700002802349700002202377700001902399700002102418700002002439856011902459 2015 eng d a0032-093500aStructural features of diverse Pin-II proteinase inhibitor genes from capsicum annuum0 aStructural features of diverse PinII proteinase inhibitor genes  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcFEB a319-3310 v2413 a

The proteinase inhibitor (PI) genes from Capsicum annuum were characterized with respect to their UTR, introns and promoter elements. The occurrence of PIs with circularly permuted domain organization was evident. Several potato inhibitor II (Pin-II) type proteinase inhibitor (PI) genes have been analyzed from Capsicum annuum (L.) with respect to their differential expression during plant defense response. However, complete gene characterization of any of these C. annuum PIs (CanPIs) has not been carried out so far. Complete gene architectures of a previously identified CanPI-7 (Beads-on-string, Type A) and a member of newly isolated Bracelet type B, CanPI-69 are reported in this study. The 5' UTR (untranslated region), 3'UTR, and intronic sequences of both the CanPI genes were obtained. The genomic sequence of CanPI-7 exhibited, exon 1 (49 base pair, bp) and exon 2 (740 bp) interrupted by a 294-bp long type I intron. We noted the occurrence of three multi-domain PIs (CanPI-69, 70, 71) with circularly permuted domain organization. CanPI-69 was found to possess exon 1 (49 bp), exon 2 (551 bp) and a 584-bp long type I intron. The upstream sequence analysis of CanPI-7 and CanPI-69 predicted various transcription factor-binding sites including TATA and CAAT boxes, hormone-responsive elements (ABRELATERD1, DOFCOREZM, ERELEE4), and a defense-responsive element (WRKY71OS). Binding of transcription factors such as zinc finger motif MADS-box and MYB to the promoter regions was confirmed using electrophoretic mobility shift assay followed by mass spectrometric identification. The 3' UTR analysis for 25 CanPI genes revealed unique/distinct 3' UTR sequence for each gene. Structures of three domain CanPIs of type A and B were predicted and further analyzed for their attributes. This investigation of CanPI gene architecture will enable the better understanding of the genetic elements present in CanPIs.

10aCanPI10aCapsicum10aGene architecture10aPromoter10aProteinase inhibitor1 aMahajan, Neha, S.1 aDewangan, Veena1 aLomate, Purushottam, R.1 aJoshi, Rakesh, S.1 aMishra, Manasi1 aGupta, Vidya, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/structural-features-diverse-pin-ii-proteinase-inhibitor-genes-capsicum-annuum-002652nas a2200373 4500008004100000022001400041245014200055210006900197260006700266300001400333490000700347520139300354653001301747653002301760653001701783653000801800653003101808653001501839100002001854700001701874700002601891700002601917700002001943700002301963700002501986700001602011700001302027700003402040700002402074700002002098700001602118700002102134856012302155 2016 eng d a1467-764400aFusarium oxysporum mediates systems metabolic reprogramming of chickpea roots as revealed by a combination of proteomics and metabolomics0 aFusarium oxysporum mediates systems metabolic reprogramming of c a111 RIVER ST, HOBOKEN 07030-5774, NJ USAbWILEY-BLACKWELLcJUL a1589-16030 v143 a

Molecular changes elicited by plants in response to fungal attack and how this affects plant-pathogen interaction, including susceptibility or resistance, remain elusive. We studied the dynamics in root metabolism during compatible and incompatible interactions between chickpea and Fusarium oxysporum f. sp. ciceri (Foc), using quantitative label-free proteomics and NMR-based metabolomics. Results demonstrated differential expression of proteins and metabolites upon Foc inoculations in the resistant plants compared with the susceptible ones. Additionally, expression analysis of candidate genes supported the proteomic and metabolic variations in the chickpea roots upon Foc inoculation. In particular, we found that the resistant plants revealed significant increase in the carbon and nitrogen metabolism; generation of reactive oxygen species (ROS), lignification and phytoalexins. The levels of some of the pathogenesis-related proteins were significantly higher upon Foc inoculation in the resistant plant. Interestingly, results also exhibited the crucial role of altered Yang cycle, which contributed in different methylation reactions and unfolded protein response in the chickpea roots against Foc. Overall, the observed modulations in the metabolic flux as outcome of several orchestrated molecular events are determinant of plant's role in chickpea-Foc interactions.

10aChickpea10afusarium oxysporum10aMetabolomics10aNMR10aplant-pathogen interaction10aproteomics1 aKumar, Yashwant1 aZhang, Limin1 aPanigrahi, Priyabrata1 aDholakia, Bhushan, B.1 aDewangan, Veena1 aChavan, Sachin, G.1 aKunjir, Shrikant, M.1 aWu, Xiangyu1 aLi, Ning1 aRajmohanan, Pattuparambil, R.1 aKadoo, Narendra, Y.1 aGiri, Ashok, P.1 aTang, Huiru1 aGupta, Vidya, S. uhttps://library.ncl.res.in/content/fusarium-oxysporum-mediates-systems-metabolic-reprogramming-chickpea-roots-revealed02264nas a2200301 4500008004100000022001400041245011700055210006900172260009000241300002600331490000600357520118200363100002401545700002701569700001901596700002701615700002001642700002001662700001401682700001601696700002001712700002101732700002001753700002001773700001801793700001901811856013201830 2016 eng d a2041-172300aGAME9 regulates the biosynthesis of steroidal alkaloids and upstream isoprenoids in the plant mevalonate pathway0 aGAME9 regulates the biosynthesis of steroidal alkaloids and upst aMACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLANDbNATURE PUBLISHING GROUPcFEB aArticle Number: 106540 v73 a

Steroidal glycoalkaloids (SGAs) are cholesterol-derived molecules produced by solanaceous species. They contribute to pathogen defence but are toxic to humans and considered as anti-nutritional compounds. Here we show that GLYCOALKALOID METABOLISM 9 (GAME9), an APETALA2/Ethylene Response Factor, related to regulators of alkaloid production in tobacco and Catharanthus roseus, controls SGA biosynthesis. GAME9 knockdown and overexpression in tomato and potato alters expression of SGAs and upstream mevalonate pathway genes including the cholesterol biosynthesis gene STEROL SIDE CHAIN REDUCTASE 2 (SSR2). Levels of SGAs, C24-alkylsterols and the upstream mevalonate and cholesterol pathways intermediates are modified in these plants. Delta(7)-STEROL-C5(6)-DESATURASE (C5-SD) in the hitherto unresolved cholesterol pathway is a direct target of GAME9. Transactivation and promoter-binding assays show that GAME9 exerts its activity either directly or cooperatively with the SlMYC2 transcription factor as in the case of the C5-SD gene promoter. Our findings provide insight into the regulation of SGA biosynthesis and means for manipulating these metabolites in crops.

1 aCardenas, Pablo, D.1 aSonawane, Prashant, D.1 aPollier, Jacob1 aBossche, Robin, Vanden1 aDewangan, Veena1 aWeithorn, Efrat1 aTal, Lior1 aMeir, Sagit1 aRogachev, Ilana1 aMalitsky, Sergey1 aGiri, Ashok, P.1 aGoossens, Alain1 aBurdman, Saul1 aAharoni, Asaph uhttps://library.ncl.res.in/content/game9-regulates-biosynthesis-steroidal-alkaloids-and-upstream-isoprenoids-plant-mevalonate-102197nas a2200229 4500008004100000245018300041210006900224260000800293300001400301490000700315520133000322100002801652700002001680700002201700700002001722700002301742700001301765700001801778700002101796700002001817856013001837 2018 eng d00aIntegrated transcriptomic and proteomic analyses suggest the participation of endogenous protease inhibitors in the regulation of protease gene expression in helicoverpa armigera0 aIntegrated transcriptomic and proteomic analyses suggest the par cJUL a1324-13360 v173 aInsects adapt to plant protease inhibitors (PIs) present in their diet by differentially regulating multiple digestive proteases. However, mechanisms regulating protease gene expression in insects are largely enigmatic. Ingestion of multi-domain recombinant Capsicum annuum protease inhibitor-7 (CanPI-7) arrests growth and development of Helicoverpa armigera (Lepidoptera: Noctuidae). Using de novo RNA sequencing and proteomic analysis, we examined the response of H. armigera larvae fed on recombinant CanPI-7 at different time intervals. Here, we present evidence supporting a dynamic transition in H. armigera protease expression on CanPI-7 feeding with general down-regulation of protease genes at early time points (0.5 to 6 h) and significant up-regulation of specific trypsin, chymotrypsin and aminopeptidase genes at later time points (12 to 48 h). Further, coexpression of H. armigera endogenous PIs with several digestive protease genes were apparent. In addition to the differential expression of endogenous H. armigera PIs, we also observed a distinct novel isoform of endogenous PI in CanPI-7 fed H. armigera larvae. Based on present and earlier studies, we propose potential mechanism of protease regulation in H. armigera and subsequent adaptation strategy to cope with anti-nutritional components of plants.1 aLomate, Purushottam, R.1 aDewangan, Veena1 aMahajan, Neha, S.1 aKumar, Yashwant1 aKulkarni, Abhijeet1 aWang, Li1 aSaxena, Smita1 aGupta, Vidya, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/integrated-transcriptomic-and-proteomic-analyses-suggest-participation-endogenous-protease