ArticlePlant molecular biology2006
Direct interaction between the tobacco mosaic virus helicase domain and the ATP-bound resistance protein, N factor during the hypersensitive response in tobacco plants.
Article in Plant molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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66 citing papers in PubMed, 177 citations in OpenAlex.
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- Plant Immunity against Tobamoviruses.Viruses · 2024Review
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- Signaling and Resistosome Formation in Plant Innate Immunity to Viruses: Is There a Common Mechanism of Antiviral Resistance Conserved across Kingdoms?International journal of molecular sciences · 2023Review
- The Secret Life of the Inhibitor of Virus Replication.Viruses · 2022Article
- Direct recognition of pathogen effectors by plant NLR immune receptors and downstream signalling.Essays in biochemistry · 2022Review
- Transcriptional Programs and Regulators Underlying Age-Dependent and Dark-Induced Senescence inCells · 2022Article
- Stepwise artificial evolution of an Sw-5b immune receptor extends its resistance spectrum against resistance-breaking isolates of Tomato spotted wilt virus.Plant biotechnology journal · 2021Article
- In silico modelling and characterization of eight blast resistance proteins in resistant and susceptible rice cultivars.Journal, genetic engineering & biotechnology · 2020Article
- Perspectives on intracellular perception of plant viruses.Molecular plant pathology · 2019Review
- Transgressive segregation reveals mechanisms ofProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Binding studies between cytosinpeptidemycin and the superfamily 1 helicase protein of tobacco mosaic virus.RSC advances · 2018Article
- Plant STAND P-loop NTPases: a current perspective of genome distribution, evolution, and function : Plant STAND P-loop NTPases: genomic organization, evolution, and molecular mechanism models contribute broadly to plant pathogen defense.Molecular genetics and genomics : MGG · 2018Review
- The Coiled-Coil and Nucleotide Binding Domains of BROWN PLANTHOPPER RESISTANCE14 Function in Signaling and Resistance against Planthopper in Rice.The Plant cell · 2017Article
- Plant immunity against viruses: antiviral immune receptors in focus.Annals of botany · 2017Review
- Hairpin RNA Targeting Multiple Viral Genes Confers Strong Resistance to Rice Black-Streaked Dwarf Virus.International journal of molecular sciences · 2016Article
- Comparative analysis of plant immune receptor architectures uncovers host proteins likely targeted by pathogens.BMC biology · 2016Article
- Cross-Talk in Viral Defense Signaling in Plants.Frontiers in microbiology · 2016Review
6 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plants cope with pathogens with distinct mechanisms. One example is a gene-for-gene system, in which plants recognize the pathogen molecule by specified protein(s), this being called the R factor. However, mechanisms of interaction between proteins from the host and the pathogen are not completely understood. Here, we analyzed the mode of interaction between the N factor, a tobacco R factor, and the helicase domain (p50) of tobacco mosaic virus (TMV). To this end, domain dissected proteins were prepared and subjected to Agroinfiltration into intact leaves, followed by yeast two hybrid and pull-down assays. The results pointed to three novel features. First, the N factor was found to directly bind to the p50 of TMV, second, ATP was pre-requisite for this interaction, with formation of an ATP/N factor complex, and third, the N factor was shown to possess ATPase activity, which is enhanced by the p50. Moreover, we found that intra- and/or inter-molecular interactions take place in the N factor molecule. This interaction required ATP, and was disrupted by the p50. Based on these results, we propose a following model for the TMV recognition mechanism in tobacco plants. The N factor forms a complex with ATP, to which the helicase domain interacts, and enhances ATP hydrolysis. The resulting ADP/N factor complex then changes its conformation, thereby facilitating further interaction with the down-stream signaling factor(s). This model is consistent with the idea of 'protein machine'.
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