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Maize Homologs of Hydroxycinnamoyltransferase, a Key Enzyme in Lignin Biosynthesis, Bind the Nucleotide Binding Leucine-Rich Repeat Rp1 Proteins to Modulate the Defense Response

Guan-Feng Wang, Yijian He, Renee Strauch, Bode A. Olukolu, Dahlia Nielsen, Xu Li, Peter J. Balint-Kurti
Guan-Feng Wang
Departments of Plant Pathology (G.-F.W., Y.H., B.A.O., P.J.B.-K.),
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  • For correspondence: gwang11@ncsu.edu peter.balint-kurti@ars.usda.gov
Yijian He
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Renee Strauch
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Bode A. Olukolu
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Dahlia Nielsen
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Xu Li
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Peter J. Balint-Kurti
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  • For correspondence: gwang11@ncsu.edu peter.balint-kurti@ars.usda.gov

Published November 2015. DOI: https://doi.org/10.1104/pp.15.00703

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  • © 2015 American Society of Plant Biologists. All Rights Reserved.

Abstract

In plants, most disease resistance genes encode nucleotide binding Leu-rich repeat (NLR) proteins that trigger a rapid localized cell death called a hypersensitive response (HR) upon pathogen recognition. The maize (Zea mays) NLR protein Rp1-D21 derives from an intragenic recombination between two NLRs, Rp1-D and Rp1-dp2, and confers an autoactive HR in the absence of pathogen infection. From a previous quantitative trait loci and genome-wide association study, we identified a single-nucleotide polymorphism locus highly associated with variation in the severity of Rp1-D21-induced HR. Two maize genes encoding hydroxycinnamoyltransferase (HCT; a key enzyme involved in lignin biosynthesis) homologs, termed HCT1806 and HCT4918, were adjacent to this single-nucleotide polymorphism. Here, we show that both HCT1806 and HCT4918 physically interact with and suppress the HR conferred by Rp1-D21 but not other autoactive NLRs when transiently coexpressed in Nicotiana benthamiana. Other maize HCT homologs are unable to confer the same level of suppression on Rp1-D21-induced HR. The metabolic activity of HCT1806 and HCT4918 is unlikely to be necessary for their role in suppressing HR. We show that the lignin pathway is activated by Rp1-D21 at both the transcriptional and metabolic levels. We derive a model to explain the roles of HCT1806 and HCT4918 in Rp1-mediated disease resistance.

  • Glossary

    BiFC
    bimolecular fluorescence complementation
    cDNA
    complementary DNA
    Co-IP
    coimmunoprecipitation
    HR
    hypersensitive response
    LD
    linkage disequilibrium
    MAMP
    microbe-associated molecular pattern
    NAM
    nested association mapping
    RNA-Seq
    RNA-sequencing
    SA
    salicylic acid
    SNP
    single-nucleotide polymorphism
    • Received May 16, 2015.
    • Accepted September 8, 2015.
    • Published September 15, 2015.
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    Maize Homologs of Hydroxycinnamoyltransferase, a Key Enzyme in Lignin Biosynthesis, Bind the Nucleotide Binding Leucine-Rich Repeat Rp1 Proteins to Modulate the Defense Response
    Guan-Feng Wang, Yijian He, Renee Strauch, Bode A. Olukolu, Dahlia Nielsen, Xu Li, Peter J. Balint-Kurti
    Plant Physiology Nov 2015, 169 (3) 2230-2243; DOI: 10.1104/pp.15.00703

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    Maize Homologs of Hydroxycinnamoyltransferase, a Key Enzyme in Lignin Biosynthesis, Bind the Nucleotide Binding Leucine-Rich Repeat Rp1 Proteins to Modulate the Defense Response
    Guan-Feng Wang, Yijian He, Renee Strauch, Bode A. Olukolu, Dahlia Nielsen, Xu Li, Peter J. Balint-Kurti
    Plant Physiology Nov 2015, 169 (3) 2230-2243; DOI: 10.1104/pp.15.00703
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    Plant Physiology: 169 (3)
    Plant Physiology
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    Nov 2015
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