Ubiquitin ligase-associated protein SGT1 is required for host and nonhost disease resistance in plants

Jack R. Peart; Rui Lu; Ari Sadanandom; Isabelle Malcuit; Peter Moffett; David C. Brice; Leif Schauser; Daniel A. W. Jaggard; Shunyuan Xiao; Mark J. Coleman; Max Dow; Jonathan D. G. Jones; Ken Shirasu; David C. Baulcombe

doi:10.1073/pnas.152330599

Ubiquitin ligase-associated protein SGT1 is required for host and nonhost disease resistance in plants

Jack R. Peart, Rui Lu, Ari Sadanandom, Isabelle Malcuit, Peter Moffett, David C. Brice, Leif Schauser, Daniel A. W. Jaggard, Shunyuan Xiao, Mark J. Coleman, Max Dow, Jonathan D. G. Jones, Ken Shirasu, David C. Baulcombe

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371 Citations (Scopus)

Abstract

Homologues of the yeast ubiquitin ligase-associated protein SGT1 are required for disease resistance in plants mediated by nucleotide-binding site/leucine-rich repeat (NBS-LRR) proteins. Here, by silencing SGT1 in Nicotiana benthamiana, we extend these findings and demonstrate that SGT1 has an unexpectedly general role in disease resistance. It is required for resistance responses mediated by NBS-LRR and other R proteins in which pathogen-derived elicitors are recognized either inside or outside the host plant cell. A requirement also exists for SGT1 in nonhost resistance in which all known members of a host species are resistant against every characterized isolate of a pathogen. Our findings show that silencing SGT1 affects diverse types of disease resistance in plants and support the idea that R protein-mediated and nonhost resistance may involve similar mechanisms.

Original language	English
Pages (from-to)	10865-10869
Number of pages	5
Journal	Proceedings of the National Academy of Sciences USA
Volume	99
Issue number	16
DOIs	https://doi.org/10.1073/pnas.152330599
Publication status	Published - 6 Aug 2002

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10.1073/pnas.152330599

Cite this

Peart, J. R., Lu, R., Sadanandom, A., Malcuit, I., Moffett, P., Brice, D. C., Schauser, L., Jaggard, D. A. W., Xiao, S., Coleman, M. J., Dow, M., Jones, J. D. G., Shirasu, K., & Baulcombe, D. C. (2002). Ubiquitin ligase-associated protein SGT1 is required for host and nonhost disease resistance in plants. Proceedings of the National Academy of Sciences USA, 99(16), 10865-10869. https://doi.org/10.1073/pnas.152330599

@article{f13c0615a6fb4f39a30de0c0b177862a,

title = "Ubiquitin ligase-associated protein SGT1 is required for host and nonhost disease resistance in plants",

abstract = "Homologues of the yeast ubiquitin ligase-associated protein SGT1 are required for disease resistance in plants mediated by nucleotide-binding site/leucine-rich repeat (NBS-LRR) proteins. Here, by silencing SGT1 in Nicotiana benthamiana, we extend these findings and demonstrate that SGT1 has an unexpectedly general role in disease resistance. It is required for resistance responses mediated by NBS-LRR and other R proteins in which pathogen-derived elicitors are recognized either inside or outside the host plant cell. A requirement also exists for SGT1 in nonhost resistance in which all known members of a host species are resistant against every characterized isolate of a pathogen. Our findings show that silencing SGT1 affects diverse types of disease resistance in plants and support the idea that R protein-mediated and nonhost resistance may involve similar mechanisms.",

author = "Peart, {Jack R.} and Rui Lu and Ari Sadanandom and Isabelle Malcuit and Peter Moffett and Brice, {David C.} and Leif Schauser and Jaggard, {Daniel A. W.} and Shunyuan Xiao and Coleman, {Mark J.} and Max Dow and Jones, {Jonathan D. G.} and Ken Shirasu and Baulcombe, {David C.}",

year = "2002",

month = aug,

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doi = "10.1073/pnas.152330599",

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Peart, JR, Lu, R, Sadanandom, A, Malcuit, I, Moffett, P, Brice, DC, Schauser, L, Jaggard, DAW, Xiao, S, Coleman, MJ, Dow, M, Jones, JDG, Shirasu, K & Baulcombe, DC 2002, 'Ubiquitin ligase-associated protein SGT1 is required for host and nonhost disease resistance in plants', Proceedings of the National Academy of Sciences USA, vol. 99, no. 16, pp. 10865-10869. https://doi.org/10.1073/pnas.152330599

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T1 - Ubiquitin ligase-associated protein SGT1 is required for host and nonhost disease resistance in plants

AU - Peart, Jack R.

AU - Lu, Rui

AU - Sadanandom, Ari

AU - Malcuit, Isabelle

AU - Moffett, Peter

AU - Brice, David C.

AU - Schauser, Leif

AU - Jaggard, Daniel A. W.

AU - Xiao, Shunyuan

AU - Coleman, Mark J.

AU - Dow, Max

AU - Jones, Jonathan D. G.

AU - Shirasu, Ken

AU - Baulcombe, David C.

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N2 - Homologues of the yeast ubiquitin ligase-associated protein SGT1 are required for disease resistance in plants mediated by nucleotide-binding site/leucine-rich repeat (NBS-LRR) proteins. Here, by silencing SGT1 in Nicotiana benthamiana, we extend these findings and demonstrate that SGT1 has an unexpectedly general role in disease resistance. It is required for resistance responses mediated by NBS-LRR and other R proteins in which pathogen-derived elicitors are recognized either inside or outside the host plant cell. A requirement also exists for SGT1 in nonhost resistance in which all known members of a host species are resistant against every characterized isolate of a pathogen. Our findings show that silencing SGT1 affects diverse types of disease resistance in plants and support the idea that R protein-mediated and nonhost resistance may involve similar mechanisms.

AB - Homologues of the yeast ubiquitin ligase-associated protein SGT1 are required for disease resistance in plants mediated by nucleotide-binding site/leucine-rich repeat (NBS-LRR) proteins. Here, by silencing SGT1 in Nicotiana benthamiana, we extend these findings and demonstrate that SGT1 has an unexpectedly general role in disease resistance. It is required for resistance responses mediated by NBS-LRR and other R proteins in which pathogen-derived elicitors are recognized either inside or outside the host plant cell. A requirement also exists for SGT1 in nonhost resistance in which all known members of a host species are resistant against every characterized isolate of a pathogen. Our findings show that silencing SGT1 affects diverse types of disease resistance in plants and support the idea that R protein-mediated and nonhost resistance may involve similar mechanisms.

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DO - 10.1073/pnas.152330599

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