03296nas a2200277 4500008004100000022001400041245007100055210006900126260008100195300000800276490000700284520235500291653001002646653001402656653002002670653003802690653002902728100001902757700002202776700002802798700002502826700002102851700002102872700002002893856010502913 2012 eng d a1471-222900aStress inducible proteinase inhibitor diversity in capsicum annuum0 aStress inducible proteinase inhibitor diversity in capsicum annu a236 GRAYS INN RD, FLOOR 6, LONDON WC1X 8HL, ENGLANDbBIOMED CENTRAL LTDcNOV a2170 v123 a

Background: Wound-inducible Pin-II Proteinase inhibitors (PIs) are one of the important plant serine PIs which have been studied extensively for their structural and functional diversity and relevance in plant defense against insect pests. To explore the functional specialization of an array of Capsicum annuum (L.) proteinase inhibitor (CanPIs) genes, we studied their expression, processing and tissue-specific distribution under steady-state and induced conditions. Inductions were performed by subjecting C. annuum leaves to various treatments, namely aphid infestation or mechanical wounding followed by treatment with either oral secretion (OS) of Helicoverpa armigera or water. Results: The elicitation treatments regulated the accumulation of CanPIs corresponding to 4-, 3-, and 2-inhibitory repeat domains (IRDs). Fourty seven different CanPI genes composed of 28 unique IRDs were identified in total along with those reported earlier. The CanPI gene pool either from uninduced or induced leaves was dominated by 3-IRD PIs and trypsin inhibitory domains. Also a major contribution by 4-IRD CanPI genes possessing trypsin and chymotrypsin inhibitor domains was specifically revealed in wounded leaves treated with OS. Wounding displayed the highest number of unique CanPIs while wounding with OS treatment resulted in the high accumulation of specifically CanPI-4, -7 and -10. Characterization of the PI protein activity through two dimensional gel electrophoresis revealed tissue and induction specific patterns. Consistent with transcript abundance, wound plus OS or water treated C. annuum leaves exhibited significantly higher PI activity and isoform diversity contributed by 3- and 4-IRD CanPIs. CanPI accumulation and activity was weakly elicited by aphid infestation yet resulted in the higher expression of CanPI-26, -41 and -43. Conclusions: Plants can differentially perceive various kinds of insect attacks and respond appropriately through activating plant defenses including regulation of PIs at transcriptional and post-translational levels. Based on the differentially elicited CanPI accumulation patterns, it is intriguing to speculate that generating sequence diversity in the form of multi-IRD PIs is a part of elaborative plant defense strategy to obtain a diverse pool of functional units to confine insect attack.

10aCanPI10aHerbivory10aOral secretions10aPin-II type proteinase inhibitors10aPlant-insect interaction1 aMishra, Manasi1 aMahajan, Neha, S.1 aTamhane, Vaijayanti, A.1 aKulkarni, Mahesh, J.1 aBaldwin, Ian, T.1 aGupta, Vidya, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/stress-inducible-proteinase-inhibitor-diversity-capsicum-annuum-002054nas a2200253 4500008004100000022001400041245009800055210006900153260009500222300001400317490000800331520110600339653001001445653002301455653002201478653003901500653002201539100001901561700002201580700002501602700002101627700002001648856013201668 2013 eng d a0006-291X00aStructural-functional insights of single and multi-domain capsicum annuum protease inhibitors0 aStructuralfunctional insights of single and multidomain capsicum a525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USAbACADEMIC PRESS INC ELSEVIER SCIENCEcJAN a1060-10650 v4303 a

Pin-II protease inhibitors (PIs) are the focus of research interest because of their large structural-functional diversity and relevance in plant defense. Two representative Capsicum annuum PI genes (CanPI-15 and -7) comprising one and four inhibitory repeat domains, respectively, were expressed and recombinant proteins were characterized. beta-Sheet and unordered structure was found predominant in CanPI-15 while -7 also displayed the signatures of polyproline fold, as revealed by circular dichroism studies. Inhibition kinetics against bovine typsin indicated three times higher potency of CanPI-7 (K-i similar to 57 mu M) than -15 (similar to 184 mu M). Activity and structural stability of these CanPIs were revealed under various conditions of pH, temperature and denaturing agent. Structure prediction, docking studies with proteases and mass spectroscopy revealed the organization of multiple reactive site loops of multi domain PIs in space as well as the steric hindrances imposed while binding to proteases due to their close proximity. (C) 2012 Elsevier Inc. All rights reserved.

10aCanPI10aCircular dichroism10aDisulfide bonding10aPotato type-II protease inhibitors10aProtein stability1 aMishra, Manasi1 aJoshi, Rakesh, S.1 aGaikwad, Sushama, M.1 aGupta, Vidya, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/structural-functional-insights-single-and-multi-domain-capsicum-annuum-protease-inhibitors-002056nas a2200229 4500008004100000022001400041245006500055210006500120260010300185300001200288490000700300520125600307653002001563653002101583653001301604100002201617700001901639700002801658700002101686700002001707856009901727 2014 eng d a0981-942800aStress inducible proteomic changes in capsicum annuum leaves0 aStress inducible proteomic changes in capsicum annuum leaves a23 RUE LINOIS, 75724 PARIS, FRANCEbELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIERcJAN a212-2170 v743 a

Herbivore attack induces defense responses in plants, activating several signaling cascades. As a result, molecules deterrent to the herbivores are produced and accumulated in plants. Expression of defense mechanism/traits requires reorganization of the plant metabolism, redirecting the resources otherwise meant for growth. In the present work, protein profile of Capsicum annuum leaves was examined after herbivore attack/induction. Majority of proteins identified as differentially accumulated, were having roles in redox metabolism and photosynthesis. For example, superoxide dismutase and NADP oxidoreductase were upregulated by 10- and 6-fold while carbonic anhydrase and fructose-1,6-bisphosphatase were downregulated by 9- and 4-fold, respectively. Also, superoxide dismutase, NADPH quinone oxidoreductase and NADP dependent isocitrate dehydrogenase transcripts showed a higher accumulation in induced leaf tissues at early time points. In general, proteins having role in defense and damage repair were upregulated while those involved in photosynthesis appeared downregulated. Thus metabolic reconfiguration to balance defense and tolerance was evident in the stress-induced leaves. (C) 2013 Elsevier Masson SAS. All rights reserved.

10aCapsicum annuum10aOxidative stress10aWounding1 aMahajan, Neha, S.1 aMishra, Manasi1 aTamhane, Vaijayanti, A.1 aGupta, Vidya, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/stress-inducible-proteomic-changes-capsicum-annuum-leaves-002856nas 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-0