02424nas a2200241   4500008004100000022001400041245014400055210006900199260009500268300001200363490000800375520148000383653001601863653003001879653002301909653001001932100002201942700002301964700002401987700002102011700002002032856013002052       2014                        eng d  a0006-291X00aResistance through inhibition: ectopic expression of serine protease inhibitor offers stress tolerance via delayed senescence in yeast cell0 aResistance through inhibition ectopic expression of serine prote  a525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USAbACADEMIC PRESS INC ELSEVIER SCIENCEcSEP  a361-3680 v4523 a<p>Protease inhibitors have been known to confer multiple stress tolerance in transgenic plants. We have assessed growth of yeast (Pichia pastoris GS115) strains expressing inhibitory repeat domains (PpIRD(+)) of previously characterized Capsicum annuum protease inhibitors under high salt, heavy metal and oxidative stress. PpIRD(+) strains exhibited multiple stress tolerance and showed differential molecular responses at transcriptional and translational level on exposure to stress inducing agents like heavy metal, high salt and H2O2. PpIRD(+) strains display significant reduction in metacaspase (Yca1) activity, the key enzyme in apoptosis, indicates the possibility of cross reactivity of IRDs (serine protease inhibitor) with cysteine proteases. PpIRD(+) and Saccharomyces cerevisiae knockout with Yca1 (Delta Yca1) strain showed similar growth characteristics under stress, which indicated the delayed senescence due to cellular metacaspase inhibition. Molecular docking study showed a close proximity of IRDs reactive site and the active site of metacaspase in the complex that signified their strong interactions. Maintenance of GAPDH activity, primary target of metacaspase, in PpIRD(+) strain evidenced the inhibition of metacaspase activity and survival of these cells under stress. This report demonstrates a potential molecular mechanism of protease inhibitor-based multiple stress tolerance in yeast strains. (C) 2014 Elsevier Inc. All rights reserved.</p>10aMetacaspase10aMultiple stress tolerance10aprotease inhibitor10aYeast1 aJoshi, Rakesh, S.1 aTanpure, Rahul, S.1 aSingh, Rajan, Kumar1 aGupta, Vidya, S.1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/resistance-through-inhibition-ectopic-expression-serine-protease-inhibitor-offers-stress-002128nas a2200289   4500008004100000022001400041245013100055210006900186260007100255300001600326490000700342520109100349653001701440653002501457653002601482653002301508100002201531700001701553700001501570700002201585700001701607700002301624700002201647700002101669700002001690856012801710       2014                        eng d  a0021-856100aWay toward ``dietary pesticides'': molecular investigation of insecticidal action of caffeic acid against helicoverpa armigera0 aWay toward dietary pesticides molecular investigation of insecti  a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcNOV  a10847-108540 v623 a<p>Bioprospecting of natural molecules is essential to overcome serious environmental issues and pesticide resistance in insects. Here we are reporting insights into insecticidal activity of a plant natural phenol. In silico and in vitro screening of multiple molecules supported by in vivo validations suggested that caffeic acid (CA) is a potent inhibitor of Helicoverpa armigera gut proteases. Protease activity and gene expression were altered in CA-fed larvae. The structure-activity relationship of CA highlighted that all the functional groups are crucial for inhibition of protease activity. Biophysical studies and molecular dynamic simulations revealed that sequential binding of multiple CA molecules induces conformational changes in the protease(s) and thus lead to a significant decline in their activity. CA treatment significantly inhibits the insect's detoxification enzymes, thus intensifying the insecticidal effect. Our findings suggest that CA can be implicated as a potent insecticidal molecule and explored for the development of effective dietary pesticides.</p>10aCaffeic acid10aHelicoverpa armigera10ainsecticidal activity10aprotease inhibitor1 aJoshi, Rakesh, S.1 aWagh, T., P.1 aSharma, N.1 aMulani, Fayaj, A.1 aSonavane, U.1 aThulasiram, H., V.1 aJoshi, Rakesh, S.1 aGupta, Vidya, S.1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/way-toward-dietary-pesticides-molecular-investigation-insecticidal-action-caffeic-acid-0