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231225s2021 xx |||||o 00| ||eng c |
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|a 10.1016/j.jplph.2021.153376
|2 doi
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|a pubmed24n1071.xml
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|a (DE-627)NLM321319095
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|a (NLM)33571892
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|a (PII)S0176-1617(21)00015-8
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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 Zhang, Qinxue
|e verfasserin
|4 aut
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|a Two polygalacturonase-inhibiting proteins (VrPGIP) of Vigna radiata confer resistance to bruchids (Callosobruchus spp.)
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|c 2021
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 01.06.2021
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|a Date Revised 01.06.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2021 Elsevier GmbH. All rights reserved.
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|a Bruchids (Callosobruchus spp.) are destructive storage pests of mung beans (Vigna radiata). Bruchids infest mature seeds during storage and in the field causing heavy losses. Bruchid resistance in mung bean has been characterized as a dominant trait controlled by a single gene. Several independent mapping studies showed that the Br locus on chromosome 5 was a key quantitative trait loci (QTL) involved in bruchid resistance. Two polygalacturonase-inhibitor protein (PGIP) family genes, VrPGIP1 and VrPGIP2, located in the Br locus may be the primary genes responsible for bruchid resistance in mung bean but no experimental proof is available. We isolated the VrPGIP1 and VrPGIP2 genes from bruchid resistant mung bean cultivar V2802 and purified the proteins by prokaryotic expression. Both VrPGIP1 and VrPGIP2 had polygalacturonase inhibitor activity and both of the PGIP proteins conferred resistance to bruchids in an artificial seed test system. VrPGIPs can inhibit the enzyme activity of polygalacturonase present in males, females and fourth instar larvae of C. maculatus. These results demonstrated that VrPGIP1 and VrPGIP2 play a critical role in bruchid resistance probably through inhibiting polygalacturonase activity
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|a Journal Article
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|a Bruchid resistance
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|a Mungbean
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|a Polygalacturonase
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|a Polygalacturonase inhibiting proteins (PGIPs)
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|a PGIP protein, plant
|2 NLM
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|a Plant 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 Yan, Qiang
|e verfasserin
|4 aut
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|a Yuan, Xingxing
|e verfasserin
|4 aut
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| 700 |
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|a Lin, Yun
|e verfasserin
|4 aut
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|a Chen, Jingbin
|e verfasserin
|4 aut
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|a Wu, Ranran
|e verfasserin
|4 aut
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|a Xue, Chenchen
|e verfasserin
|4 aut
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|a Zhu, Yuelin
|e verfasserin
|4 aut
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| 700 |
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|a Chen, Xin
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 258-259(2021) vom: 15. März, Seite 153376
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnns
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| 773 |
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|g volume:258-259
|g year:2021
|g day:15
|g month:03
|g pages:153376
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|u http://dx.doi.org/10.1016/j.jplph.2021.153376
|3 Volltext
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|d 258-259
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