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231224s2014 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/eru266
|2 doi
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|a pubmed24n1338.xml
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|a (DE-627)NLM239678354
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|a (NLM)24980909
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
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|a Prabhu, S Ashok
|e verfasserin
|4 aut
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| 245 |
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|a Experimental and bioinformatic characterization of a recombinant polygalacturonase-inhibitor protein from pearl millet and its interaction with fungal polygalacturonases
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|c 2014
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 28.05.2015
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|a Date Revised 21.03.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © The Author 2014. Published by Oxford University Press on behalf of the Society for Experimental Biology.
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|a Polygalacturonases (PGs) are hydrolytic enzymes employed by several phytopathogens to weaken the plant cell wall by degrading homopolygalacturonan, a major constituent of pectin. Plants fight back by employing polygalacturonase-inhibitor proteins (PGIPs). The present study compared the inhibition potential of pearl millet PGIP (Pennisetum glaucum; PglPGIP1) with the known inhibition of Phaseolus vulgaris PGIP (PvPGIP2) against two PGs, the PG-II isoform from Aspergillus niger (AnPGII) and the PG-III isoform from Fusarium moniliforme (FmPGIII). The key rationale was to elucidate the relationship between the extent of sequence similarity of the PGIPs and the corresponding PG inhibition potential. First, a pearl millet pgip gene (Pglpgip1) was isolated and phylogenetically placed among monocot PGIPs alongside foxtail millet (Setaria italica). Upstream sequence analysis of Pglpgip1 identified important cis-elements responsive to light, plant stress hormones, and anoxic stress. PglPGIP1, heterologously produced in Escherichia coli, partially inhibited AnPGII non-competitively with a pH optimum between 4.0 and 4.5, and showed no inhibition against FmPGIII. Docking analysis showed that the concave surface of PglPGIP1 interacted strongly with the N-terminal region of AnPGII away from the active site, whereas it weakly interacted with the C-terminus of FmPGIII. Interestingly, PglPGIP1 and PvPGIP2 employed similar motif regions with few identical amino acids for interaction with AnPGII at non-substrate-binding sites; however, they engaged different regions of AnPGII. Computational mutagenesis predicted D126 (PglPGIP1)-K39 (AnPGII) to be the most significant binding contact in the PglPGIP1-AnPGII complex. Such protein-protein interaction studies are crucial in the future generation of designer host proteins for improved resistance against ever-evolving pathogen virulence factors
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Computational mutagenesis
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|a PGIPs
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4 |
|a PGs
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|a Phaseolus vulgaris
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| 650 |
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|a electrostatic surface potential
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| 650 |
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|a inhibition studies
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| 650 |
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|a pearl millet
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| 650 |
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|a protein modelling and docking.
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| 650 |
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|a Fungal Proteins
|2 NLM
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| 650 |
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|a PGIP protein, plant
|2 NLM
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| 650 |
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|a Plant Proteins
|2 NLM
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| 650 |
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|a Recombinant Proteins
|2 NLM
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| 650 |
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|a Polygalacturonase
|2 NLM
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| 650 |
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|a EC 3.2.1.15
|2 NLM
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| 700 |
1 |
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|a Singh, Ratna
|e verfasserin
|4 aut
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| 700 |
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|a Kolkenbrock, Stephan
|e verfasserin
|4 aut
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| 700 |
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|a Sujeeth, Neerakkal
|e verfasserin
|4 aut
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| 700 |
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|a El Gueddari, Nour Eddine
|e verfasserin
|4 aut
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| 700 |
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|a Moerschbacher, Bruno M
|e verfasserin
|4 aut
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| 700 |
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|a Kini, Ramachandra K
|e verfasserin
|4 aut
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| 700 |
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|a Wagenknecht, Martin
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 65(2014), 17 vom: 30. Sept., Seite 5033-47
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
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|g volume:65
|g year:2014
|g number:17
|g day:30
|g month:09
|g pages:5033-47
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|u http://dx.doi.org/10.1093/jxb/eru266
|3 Volltext
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|d 65
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|e 17
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|h 5033-47
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