Evidence map›Paper›PMID 27208251›Full record

ArticlePlant physiology2016

Maize Homologs of CCoAOMT and HCT, Two Key Enzymes in Lignin Biosynthesis, Form Complexes with the NLR Rp1 Protein to Modulate the Defense Response.

Guan-Feng Wang, Peter J Balint-Kurti

Abstract read
In one paragraph

Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

53 citing papers in PubMed.

  1. Article
  2. From Defense Executor to Engineering Target: Harnessing Lignin for Crop Resistance.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Guan-Feng WangDepartment of Plant Pathology, North Carolina State University, Raleigh, North Carolina 27695 (G.-F.W., P.J.B.-K.)Key Laboratory of Plant Cell Engineering and Germplasm Innovation, Ministry of Education, School of Life Sciences, Shandong University, Jinan, Shandong 250100, P.R. China (G.-F.W.); U.S. Department of Agriculture-Agricultural Research Service, Plant Science Research Unit, Raleigh, North Carolina 27695 (P.J.B.-K.) gfwang@sdu.edu.cn.ORCID 0000-0003-1010-2038
Peter J Balint-KurtiDepartment of Plant Pathology, North Carolina State University, Raleigh, North Carolina 27695 (G.-F.W., P.J.B.-K.)Key Laboratory of Plant Cell Engineering and Germplasm Innovation, Ministry of Education, School of Life Sciences, Shandong University, Jinan, Shandong 250100, P.R. China (G.-F.W.); U.S. Department of Agriculture-Agricultural Research Service, Plant Science Research Unit, Raleigh, North Carolina 27695 (P.J.B.-K.).ORCID 0000-0002-3916-194X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Disease resistance (R) genes encode nucleotide binding Leu-rich-repeat (NLR) proteins that confer resistance to specific pathogens. Upon pathogen recognition they trigger a defense response that usually includes a so-called hypersensitive response (HR), a rapid localized cell death at the site of pathogen infection. Intragenic recombination between two maize (Zea mays) NLRs, Rp1-D and Rp1-dp2, resulted in the formation of a hybrid NLR, Rp1-D21, which confers an autoactive HR in the absence of pathogen infection. From a previous quantitative trait loci and genome-wide association study, we identified genes encoding two key enzymes in lignin biosynthesis, hydroxycinnamoyltransferase (HCT) and caffeoyl CoA O-methyltransferase (CCoAOMT), adjacent to the nucleotide polymorphisms that were highly associated with variation in the severity of Rp1-D21-induced HR We have previously shown that the two maize HCT homologs suppress the HR conferred by Rp1-D21 in a heterologous system, very likely through physical interaction. Here, we show, similarly, that CCoAOMT2 suppresses the HR induced by either the full-length or by the N-terminal coiled-coil domain of Rp1-D21 also likely via physical interaction and that the metabolic activity of CCoAOMT2 is unlikely to be necessary for its role in suppressing HR. We also demonstrate that CCoAOMT2, HCTs, and Rp1 proteins can form in the same complexes. A model is derived to explain the roles of CCoAOMT and HCT in Rp1-mediated defense resistance.

Indexed as

AcyltransferasesDisease ResistanceGene Expression Regulation, PlantLigninMethyltransferasesMultiprotein ComplexesNicotianaNLR ProteinsPhylogenyPlant ProteinsPlants, Genetically ModifiedZea maysAcyltransferasescaffeoyl-CoA O-methyltransferaseLigninMethyltransferasesMultiprotein ComplexesNLR ProteinsPlant Proteins

Identifiers

PMID27208251
PMCPMC4936554

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.