The TIR-NBS but not LRR domains of two novel N-like proteins are functionally competent to induce the elicitor p50-dependent hypersensitive response

Jun Shan Gao, Nobumitsu Sasaki, Hiromi Kanegae, Ken ichi Konagaya, Kaori Takizawa, Naomi Hayashi, Yosuke Okano, Masahiro Kasahara, Yasuhiko Matsushita, Hiroshi Nyunoya

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The tobacco N protein recognizes the helicase domain (p50) of the Tobacco mosaic virus (TMV) replicase as an elicitor and mediates hypersensitive response (HR). We obtained two cDNA clones encoding novel N-like (NL) proteins NL-C26 and NL-B69 from Nicotiana tabacum cv. Samsun NN. NL-C26 and NL-B69 had a Toll-interleukin-1 receptor/nucleotide-binding site/leucine-rich repeat (TIR-NBS-LRR) structure and showed 78% and 73% identities to N, respectively. The NL-C26 and NL-B69 genes were also expressed in N. tabacum cv. Samsun nn, which lacks the N gene. Unlike N, NL-C26 and NL-B69, when coexpressed with p50, failed to induce HR on the sites of agroinfiltration in Samsun nn leaves. However, the elicitor-dependent HR in Samsun nn was induced efficiently by chimeric N proteins with the continuous TIR-NBS domains of NL-C26 and NL-B69. On the other hand, the efficiency of HR induction varied significantly among chimeric N proteins with either of the TIR and NBS domains of the NL proteins. In contrast, chimeras carrying the LRR domains of the NL proteins did not induce HR. Thus, the TIR-NBS domains of NL-C26 and NL-B69 could functionally adapt to the LRR domain of N, which may determine the specificity for the elicitor. We speculate that the NL genes are potential HR-inducing resistance genes for undetermined pathogens other than TMV.

Original languageEnglish
Pages (from-to)78-87
Number of pages10
JournalPhysiological and Molecular Plant Pathology
Volume71
Issue number1-3
DOIs
Publication statusPublished - 2007 Jul
Externally publishedYes

Fingerprint

hypersensitive response
Proteins
Tobacco mosaic virus
proteins
Genes
Tobacco
Nicotiana tabacum
Tobacco Mosaic Virus
genes
agroinfiltration
Interleukin-1 Receptors
Leucine
chimerism
interleukin-1
Nucleotides
Complementary DNA
Clone Cells
leucine
Binding Sites
elicitors

Keywords

  • Elicitor
  • HR
  • Hypersensitive response
  • N gene
  • N homolog
  • Nicotiana tabacum
  • Samsun

ASJC Scopus subject areas

  • Plant Science

Cite this

The TIR-NBS but not LRR domains of two novel N-like proteins are functionally competent to induce the elicitor p50-dependent hypersensitive response. / Gao, Jun Shan; Sasaki, Nobumitsu; Kanegae, Hiromi; Konagaya, Ken ichi; Takizawa, Kaori; Hayashi, Naomi; Okano, Yosuke; Kasahara, Masahiro; Matsushita, Yasuhiko; Nyunoya, Hiroshi.

In: Physiological and Molecular Plant Pathology, Vol. 71, No. 1-3, 07.2007, p. 78-87.

Research output: Contribution to journalArticle

Gao, Jun Shan ; Sasaki, Nobumitsu ; Kanegae, Hiromi ; Konagaya, Ken ichi ; Takizawa, Kaori ; Hayashi, Naomi ; Okano, Yosuke ; Kasahara, Masahiro ; Matsushita, Yasuhiko ; Nyunoya, Hiroshi. / The TIR-NBS but not LRR domains of two novel N-like proteins are functionally competent to induce the elicitor p50-dependent hypersensitive response. In: Physiological and Molecular Plant Pathology. 2007 ; Vol. 71, No. 1-3. pp. 78-87.
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abstract = "The tobacco N protein recognizes the helicase domain (p50) of the Tobacco mosaic virus (TMV) replicase as an elicitor and mediates hypersensitive response (HR). We obtained two cDNA clones encoding novel N-like (NL) proteins NL-C26 and NL-B69 from Nicotiana tabacum cv. Samsun NN. NL-C26 and NL-B69 had a Toll-interleukin-1 receptor/nucleotide-binding site/leucine-rich repeat (TIR-NBS-LRR) structure and showed 78{\%} and 73{\%} identities to N, respectively. The NL-C26 and NL-B69 genes were also expressed in N. tabacum cv. Samsun nn, which lacks the N gene. Unlike N, NL-C26 and NL-B69, when coexpressed with p50, failed to induce HR on the sites of agroinfiltration in Samsun nn leaves. However, the elicitor-dependent HR in Samsun nn was induced efficiently by chimeric N proteins with the continuous TIR-NBS domains of NL-C26 and NL-B69. On the other hand, the efficiency of HR induction varied significantly among chimeric N proteins with either of the TIR and NBS domains of the NL proteins. In contrast, chimeras carrying the LRR domains of the NL proteins did not induce HR. Thus, the TIR-NBS domains of NL-C26 and NL-B69 could functionally adapt to the LRR domain of N, which may determine the specificity for the elicitor. We speculate that the NL genes are potential HR-inducing resistance genes for undetermined pathogens other than TMV.",
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T1 - The TIR-NBS but not LRR domains of two novel N-like proteins are functionally competent to induce the elicitor p50-dependent hypersensitive response

AU - Gao, Jun Shan

AU - Sasaki, Nobumitsu

AU - Kanegae, Hiromi

AU - Konagaya, Ken ichi

AU - Takizawa, Kaori

AU - Hayashi, Naomi

AU - Okano, Yosuke

AU - Kasahara, Masahiro

AU - Matsushita, Yasuhiko

AU - Nyunoya, Hiroshi

PY - 2007/7

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N2 - The tobacco N protein recognizes the helicase domain (p50) of the Tobacco mosaic virus (TMV) replicase as an elicitor and mediates hypersensitive response (HR). We obtained two cDNA clones encoding novel N-like (NL) proteins NL-C26 and NL-B69 from Nicotiana tabacum cv. Samsun NN. NL-C26 and NL-B69 had a Toll-interleukin-1 receptor/nucleotide-binding site/leucine-rich repeat (TIR-NBS-LRR) structure and showed 78% and 73% identities to N, respectively. The NL-C26 and NL-B69 genes were also expressed in N. tabacum cv. Samsun nn, which lacks the N gene. Unlike N, NL-C26 and NL-B69, when coexpressed with p50, failed to induce HR on the sites of agroinfiltration in Samsun nn leaves. However, the elicitor-dependent HR in Samsun nn was induced efficiently by chimeric N proteins with the continuous TIR-NBS domains of NL-C26 and NL-B69. On the other hand, the efficiency of HR induction varied significantly among chimeric N proteins with either of the TIR and NBS domains of the NL proteins. In contrast, chimeras carrying the LRR domains of the NL proteins did not induce HR. Thus, the TIR-NBS domains of NL-C26 and NL-B69 could functionally adapt to the LRR domain of N, which may determine the specificity for the elicitor. We speculate that the NL genes are potential HR-inducing resistance genes for undetermined pathogens other than TMV.

AB - The tobacco N protein recognizes the helicase domain (p50) of the Tobacco mosaic virus (TMV) replicase as an elicitor and mediates hypersensitive response (HR). We obtained two cDNA clones encoding novel N-like (NL) proteins NL-C26 and NL-B69 from Nicotiana tabacum cv. Samsun NN. NL-C26 and NL-B69 had a Toll-interleukin-1 receptor/nucleotide-binding site/leucine-rich repeat (TIR-NBS-LRR) structure and showed 78% and 73% identities to N, respectively. The NL-C26 and NL-B69 genes were also expressed in N. tabacum cv. Samsun nn, which lacks the N gene. Unlike N, NL-C26 and NL-B69, when coexpressed with p50, failed to induce HR on the sites of agroinfiltration in Samsun nn leaves. However, the elicitor-dependent HR in Samsun nn was induced efficiently by chimeric N proteins with the continuous TIR-NBS domains of NL-C26 and NL-B69. On the other hand, the efficiency of HR induction varied significantly among chimeric N proteins with either of the TIR and NBS domains of the NL proteins. In contrast, chimeras carrying the LRR domains of the NL proteins did not induce HR. Thus, the TIR-NBS domains of NL-C26 and NL-B69 could functionally adapt to the LRR domain of N, which may determine the specificity for the elicitor. We speculate that the NL genes are potential HR-inducing resistance genes for undetermined pathogens other than TMV.

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KW - Hypersensitive response

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KW - N homolog

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