02054nas 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<p>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.</p>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-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<p>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.</p>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