<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Tamhane, Vaijayanti A.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author><author><style face="normal" font="default" size="100%">Kumar, Pavan</style></author><author><style face="normal" font="default" size="100%">Gupta, Vidya S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Spatial and temporal expression patterns of diverse Pin-II proteinase inhibitor genes in Capsicum annuum Linn</style></title><secondary-title><style face="normal" font="default" size="100%">Gene</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">CanPI</style></keyword><keyword><style  face="normal" font="default" size="100%">Capsicum annuum</style></keyword><keyword><style  face="normal" font="default" size="100%">Endogenous role</style></keyword><keyword><style  face="normal" font="default" size="100%">Pin-II</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant defense</style></keyword><keyword><style  face="normal" font="default" size="100%">Proteinase inhibitor</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">AUG</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1-2</style></number><publisher><style face="normal" font="default" size="100%">ELSEVIER SCIENCE BV</style></publisher><pub-location><style face="normal" font="default" size="100%">PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS</style></pub-location><volume><style face="normal" font="default" size="100%">442</style></volume><pages><style face="normal" font="default" size="100%">88-98</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Pin-II type proteinase inhibitor (PI) genes were cloned from fruit and stem tissues of Capsicum annuum L var Phule Jyoti using primers designed from reported CanPI gene sequence (AF039398). In total, 21 novel CanPIs, members of the Pin-II PI family, were identified in the study, with three isoforms of 1-inhibitory repeat domain (IRD), eight isoforms of 2-IRD), three isoforms of 3-IRD, five isoforms of 4-IRD and two partial CanPI sequences. Most of the sequences showed variation (2 to 20%) in the deduced AA sequences which were pronounced close to the reactive site loop. Expression patterns of CanPIs in the fruit and stem tissues of mature C. annuum plants were shown to vary qualitatively and quantitatively using semi-quantitative RT-PCR expression analysis. In the fruit tissue. CanPIs with different IRDs (from 1 to 4) were expressed simultaneously. In stem tissue, 1- and 2-IRD CanPIs were strongly expressed along moderate expression of 3- and 4-IRD genes. Analysis of CanPI protein activity showed a range of active forms across the tissues. CanPI expression was differentially up-regulated upon wounding and insect attack. Although infestation by aphids (Myzus persicae) and lepidopteran pests (Spodoptera litura) specifically induced 4-IRD CanPIs, virus-infected leaves did not affect CanPI expression. Analysis of CanPI protein activity indicated that the up-regulation in CanPI expression was not always correlated with increase in PI activity. Our results demonstrated that CanPI expression is regulated spatially, temporally as well as qualitatively and quantitatively. (C) 2009 Elsevier B.V. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1-2</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.266</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mishra, Manasi</style></author><author><style face="normal" font="default" size="100%">Tamhane, Vaijayanti A.</style></author><author><style face="normal" font="default" size="100%">Khandelwal, Neha</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author><author><style face="normal" font="default" size="100%">Gupta, Vidya S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Interaction of recombinant CanPIs with helicoverpa armigera gut proteases reveals their processing patterns, stability and efficiency</style></title><secondary-title><style face="normal" font="default" size="100%">Proteomics</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">CanPI</style></keyword><keyword><style  face="normal" font="default" size="100%">H. armigera gut proteases</style></keyword><keyword><style  face="normal" font="default" size="100%">Intensity fading MALDI-TOF-MS</style></keyword><keyword><style  face="normal" font="default" size="100%">Pin-II</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant proteomics</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant-insect interaction</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUL</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">15</style></number><publisher><style face="normal" font="default" size="100%">WILEY-V C H VERLAG GMBH</style></publisher><pub-location><style face="normal" font="default" size="100%">PO BOX 10 11 61, D-69451 WEINHEIM, GERMANY</style></pub-location><volume><style face="normal" font="default" size="100%">10</style></volume><pages><style face="normal" font="default" size="100%">2845-2857</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Six diverse representative Capsicum annuum (common name: hot pepper; Solanaceae) protease inhibitor genes, viz CanPI-5, -7, -13, -15, -19, and 22 comprising 1-4 inhibitory repeat domains (IRDs), were cloned and expressed in Pichia pastoris. The recombinant proteins were evaluated for their interactions with bovine trypsin, chymotrypsin, and Helicoverpa armigera gut proteases (HGP) using electrophoretic (native and denaturing) and mass spectrometric (MALDI-TOF-MS in combination with intensity fading assays) techniques. These techniques allow qualitative and semiquantitative analysis of multiple and processed IRDs of purified recombinant Capsicum annuum proteinase inhibitor (rCanPI) proteins. rCanPIs showed over 90% trypsin inhibition, varying chymotrypsin inhibition depending on the number of respective IRDs and over 60% inhibition of total HGP. rCanPI-15 that has only one IRD showed exceptionally low inhibition of these proteases. Interaction studies of rCanPIs with proteases using intensity fading-MALDI-TOF-MS revealed gradual processing of multi-IRD rCanPIs into single IRD forms by the action of HGP at the linker region, unlike their interactions with trypsin and chymotrypsin. Intensity fading-MALDI-TOF-MS assay showed that CanPI-13 and -15, possessing single IRD and expressed predominantly in stem tissue are degraded by HGP; indicating their function other than defense. In vitro and in vivo studies on rCanPI-5 and -7 showed maximum inhibition of HGP isoforms and their processed IRDs were also found to be stable in the presence of HGP. Even single amino acid variations in IRDs were found to change the HGP specificity like in the case of HGP-8 inhibited only by IRD-12. The presence of active PI in insect gut might be responsible for changed HGP profile. rCanPI-5 and -7 enhanced HGP-7, reduced HGP-4, -5, -10 expression and new protease isoforms were induced. These results signify isoform complexity in plant PIs and insect proteases.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">15</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">4.815</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mishra, Manasi</style></author><author><style face="normal" font="default" size="100%">Mahajan, Neha S.</style></author><author><style face="normal" font="default" size="100%">Tamhane, Vaijayanti A.</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author><author><style face="normal" font="default" size="100%">Baldwin, Ian T.</style></author><author><style face="normal" font="default" size="100%">Gupta, Vidya S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Stress inducible proteinase inhibitor diversity in capsicum annuum</style></title><secondary-title><style face="normal" font="default" size="100%">BMC Plant Biology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">CanPI</style></keyword><keyword><style  face="normal" font="default" size="100%">Herbivory</style></keyword><keyword><style  face="normal" font="default" size="100%">Oral secretions</style></keyword><keyword><style  face="normal" font="default" size="100%">Pin-II type proteinase inhibitors</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant-insect interaction</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><publisher><style face="normal" font="default" size="100%">BIOMED CENTRAL LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">236 GRAYS INN RD, FLOOR 6, LONDON WC1X 8HL, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">12</style></volume><pages><style face="normal" font="default" size="100%">217</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">4.354
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mishra, Manasi</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author><author><style face="normal" font="default" size="100%">Gaikwad, Sushama M.</style></author><author><style face="normal" font="default" size="100%">Gupta, Vidya S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Structural-functional insights of single and multi-domain capsicum annuum protease inhibitors</style></title><secondary-title><style face="normal" font="default" size="100%">Biochemical and Biophysical Research Communications</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">CanPI</style></keyword><keyword><style  face="normal" font="default" size="100%">Circular dichroism</style></keyword><keyword><style  face="normal" font="default" size="100%">Disulfide bonding</style></keyword><keyword><style  face="normal" font="default" size="100%">Potato type-II protease inhibitors</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein stability</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JAN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><publisher><style face="normal" font="default" size="100%">ACADEMIC PRESS INC ELSEVIER SCIENCE</style></publisher><pub-location><style face="normal" font="default" size="100%">525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA</style></pub-location><volume><style face="normal" font="default" size="100%">430</style></volume><pages><style face="normal" font="default" size="100%">1060-1065</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.281
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mahajan, Neha S.</style></author><author><style face="normal" font="default" size="100%">Dewangan, Veena</style></author><author><style face="normal" font="default" size="100%">Lomate, Purushottam R.</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author><author><style face="normal" font="default" size="100%">Mishra, Manasi</style></author><author><style face="normal" font="default" size="100%">Gupta, Vidya S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Structural features of diverse Pin-II proteinase inhibitor genes from capsicum annuum</style></title><secondary-title><style face="normal" font="default" size="100%">Planta</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">CanPI</style></keyword><keyword><style  face="normal" font="default" size="100%">Capsicum</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene architecture</style></keyword><keyword><style  face="normal" font="default" size="100%">Promoter</style></keyword><keyword><style  face="normal" font="default" size="100%">Proteinase inhibitor</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">2</style></number><publisher><style face="normal" font="default" size="100%">SPRINGER</style></publisher><pub-location><style face="normal" font="default" size="100%">233 SPRING ST, NEW YORK, NY 10013 USA</style></pub-location><volume><style face="normal" font="default" size="100%">241</style></volume><pages><style face="normal" font="default" size="100%">319-331</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">3.239</style></custom4></record></records></xml>