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An isoleucine residue acts as a thermal and regulatory switch in wheat Rubisco activase

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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An isoleucine residue acts as a thermal and regulatory switch in wheat Rubisco activase. / Degen, Gustaf E.; Worrall, Dawn; Carmo-Silva, Elizabete.
In: The Plant Journal, Vol. 103, No. 2, 04.05.2020, p. 742-751.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Degen, GE, Worrall, D & Carmo-Silva, E 2020, 'An isoleucine residue acts as a thermal and regulatory switch in wheat Rubisco activase', The Plant Journal, vol. 103, no. 2, pp. 742-751. https://doi.org/10.1111/tpj.14766

APA

Degen, G. E., Worrall, D., & Carmo-Silva, E. (2020). An isoleucine residue acts as a thermal and regulatory switch in wheat Rubisco activase. The Plant Journal, 103(2), 742-751. Advance online publication. https://doi.org/10.1111/tpj.14766

Vancouver

Degen GE, Worrall D, Carmo-Silva E. An isoleucine residue acts as a thermal and regulatory switch in wheat Rubisco activase. The Plant Journal. 2020 May 4;103(2):742-751. Epub 2020 May 4. doi: 10.1111/tpj.14766

Author

Degen, Gustaf E. ; Worrall, Dawn ; Carmo-Silva, Elizabete. / An isoleucine residue acts as a thermal and regulatory switch in wheat Rubisco activase. In: The Plant Journal. 2020 ; Vol. 103, No. 2. pp. 742-751.

Bibtex

@article{e3fd2193e518414e8bf9f8bb7dd5f97b,
title = "An isoleucine residue acts as a thermal and regulatory switch in wheat Rubisco activase",
abstract = "The regulation of Rubisco, the gatekeeper of carbon fixation into the biosphere, by its molecular chaperone Rubisco activase (Rca) is essential for photosynthesis and plant growth. Using energy from ATP hydrolysis, Rca promotes the release of inhibitors and restores catalytic competence to Rubisco-active sites. Rca is sensitive to moderate heat stress, however, and becomes progressively inhibited as the temperature increases above the optimum for photosynthesis. Here, we identify a single amino acid substitution (M159I) that fundamentally alters the thermal and regulatory properties of Rca in bread wheat (Triticum aestivum L.). Using site-directed mutagenesis, we demonstrate that the M159I substitution extends the temperature optimum of the most abundant Rca isoform by 5°C in vitro, while maintaining the efficiency of Rubisco activation by Rca. The results suggest that this single amino acid substitution acts as a thermal and regulatory switch in wheat Rca that can be exploited to improve the climate resilience and efficiency of carbon assimilation of this cereal crop as temperatures become warmer and more volatile.",
keywords = "Rubisco, Rubisco activase, heat stress, photosynthesis, food security, wheat, Triticum aestivum",
author = "Degen, {Gustaf E.} and Dawn Worrall and Elizabete Carmo-Silva",
year = "2020",
month = may,
day = "4",
doi = "10.1111/tpj.14766",
language = "English",
volume = "103",
pages = "742--751",
journal = "The Plant Journal",
issn = "0960-7412",
publisher = "Blackwell Publishing Ltd",
number = "2",

}

RIS

TY - JOUR

T1 - An isoleucine residue acts as a thermal and regulatory switch in wheat Rubisco activase

AU - Degen, Gustaf E.

AU - Worrall, Dawn

AU - Carmo-Silva, Elizabete

PY - 2020/5/4

Y1 - 2020/5/4

N2 - The regulation of Rubisco, the gatekeeper of carbon fixation into the biosphere, by its molecular chaperone Rubisco activase (Rca) is essential for photosynthesis and plant growth. Using energy from ATP hydrolysis, Rca promotes the release of inhibitors and restores catalytic competence to Rubisco-active sites. Rca is sensitive to moderate heat stress, however, and becomes progressively inhibited as the temperature increases above the optimum for photosynthesis. Here, we identify a single amino acid substitution (M159I) that fundamentally alters the thermal and regulatory properties of Rca in bread wheat (Triticum aestivum L.). Using site-directed mutagenesis, we demonstrate that the M159I substitution extends the temperature optimum of the most abundant Rca isoform by 5°C in vitro, while maintaining the efficiency of Rubisco activation by Rca. The results suggest that this single amino acid substitution acts as a thermal and regulatory switch in wheat Rca that can be exploited to improve the climate resilience and efficiency of carbon assimilation of this cereal crop as temperatures become warmer and more volatile.

AB - The regulation of Rubisco, the gatekeeper of carbon fixation into the biosphere, by its molecular chaperone Rubisco activase (Rca) is essential for photosynthesis and plant growth. Using energy from ATP hydrolysis, Rca promotes the release of inhibitors and restores catalytic competence to Rubisco-active sites. Rca is sensitive to moderate heat stress, however, and becomes progressively inhibited as the temperature increases above the optimum for photosynthesis. Here, we identify a single amino acid substitution (M159I) that fundamentally alters the thermal and regulatory properties of Rca in bread wheat (Triticum aestivum L.). Using site-directed mutagenesis, we demonstrate that the M159I substitution extends the temperature optimum of the most abundant Rca isoform by 5°C in vitro, while maintaining the efficiency of Rubisco activation by Rca. The results suggest that this single amino acid substitution acts as a thermal and regulatory switch in wheat Rca that can be exploited to improve the climate resilience and efficiency of carbon assimilation of this cereal crop as temperatures become warmer and more volatile.

KW - Rubisco

KW - Rubisco activase

KW - heat stress

KW - photosynthesis

KW - food security

KW - wheat

KW - Triticum aestivum

U2 - 10.1111/tpj.14766

DO - 10.1111/tpj.14766

M3 - Journal article

VL - 103

SP - 742

EP - 751

JO - The Plant Journal

JF - The Plant Journal

SN - 0960-7412

IS - 2

ER -