A sleigh ride through the SNO: Regulation of plant immune function by protein S-nitrosylation

Manda Yu; Byung-Wook Yun; Steven H Spoel; Gary J Loake

doi:10.1016/j.pbi.2012.03.005

A sleigh ride through the SNO: Regulation of plant immune function by protein S-nitrosylation

Manda Yu, Byung-Wook Yun, Steven H Spoel, Gary J Loake

School of Biological Sciences

Research output: Contribution to journal › Literature review › peer-review

Abstract / Description of output

S-nitrosylation, the covalent attachment of a nitric oxide (NO) moiety to a protein cysteine thiol to form an S-nitrosothiol (SNO) is rapidly emerging as a prototypic, redox-based post-translational modification during plant immune function. Here we review recently identified targets for S-nitrosylation and the consequences of these modifications in relation to the control of plant disease resistance.

Original language	English
Journal	Current opinion in plant biology
DOIs	https://doi.org/10.1016/j.pbi.2012.03.005
Publication status	Published - Aug 2012

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10.1016/j.pbi.2012.03.005

1 Finished

Protein modification as a tool for reprogramming gene activity
Spoel, S.
Other (Learned Society)
1/10/10 → 30/09/15
Project: Research

1 Article
1 Literature review

S-nitrosylation of NADPH oxidase regulates cell death in plant immunity
Yun, B-W., Feechan, A., Yin, M., Saidi, N. B. B., Le Bihan, T., Yu, M., Moore, J. W., Kang, J-G., Kwon, E., Spoel, S. H., Pallas, J. A. & Loake, G. J., 13 Oct 2011, In: Nature. 478, 7368, p. 264-U161 7 p.
Research output: Contribution to journal › Article › peer-review
Redox-based protein modifications: The missing link in plant immune signalling
Spoel, S. H. & Loake, G. J., Aug 2011, In: Current opinion in plant biology. 14, 4, p. 358-364 7 p.
Research output: Contribution to journal › Literature review › peer-review

Cite this

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title = "A sleigh ride through the SNO: Regulation of plant immune function by protein S-nitrosylation",

abstract = "S-nitrosylation, the covalent attachment of a nitric oxide (NO) moiety to a protein cysteine thiol to form an S-nitrosothiol (SNO) is rapidly emerging as a prototypic, redox-based post-translational modification during plant immune function. Here we review recently identified targets for S-nitrosylation and the consequences of these modifications in relation to the control of plant disease resistance.",

author = "Manda Yu and Byung-Wook Yun and Spoel, {Steven H} and Loake, {Gary J}",

year = "2012",

month = aug,

doi = "10.1016/j.pbi.2012.03.005",

language = "English",

journal = "Current opinion in plant biology",

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T2 - Regulation of plant immune function by protein S-nitrosylation

AU - Yu, Manda

AU - Yun, Byung-Wook

AU - Spoel, Steven H

AU - Loake, Gary J

PY - 2012/8

Y1 - 2012/8

N2 - S-nitrosylation, the covalent attachment of a nitric oxide (NO) moiety to a protein cysteine thiol to form an S-nitrosothiol (SNO) is rapidly emerging as a prototypic, redox-based post-translational modification during plant immune function. Here we review recently identified targets for S-nitrosylation and the consequences of these modifications in relation to the control of plant disease resistance.

AB - S-nitrosylation, the covalent attachment of a nitric oxide (NO) moiety to a protein cysteine thiol to form an S-nitrosothiol (SNO) is rapidly emerging as a prototypic, redox-based post-translational modification during plant immune function. Here we review recently identified targets for S-nitrosylation and the consequences of these modifications in relation to the control of plant disease resistance.

U2 - 10.1016/j.pbi.2012.03.005

DO - 10.1016/j.pbi.2012.03.005

M3 - Literature review

C2 - 22464350

JO - Current opinion in plant biology

JF - Current opinion in plant biology

ER -

A sleigh ride through the SNO: Regulation of plant immune function by protein S-nitrosylation

Abstract / Description of output

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Projects

Protein modification as a tool for reprogramming gene activity

Research output

S-nitrosylation of NADPH oxidase regulates cell death in plant immunity

Redox-based protein modifications: The missing link in plant immune signalling

Cite this