Submitted manuscript, 1.41 MB, Word document
Rights statement: This is the peer reviewed version of the following article: Degen, G.E., Orr, D.J. and Carmo‐Silva, E. (2020), Heat‐induced changes in the abundance of wheat Rubisco activase isoforms. New Phytol. Accepted Author Manuscript. doi:10.1111/nph.16937 which has been published in final form at https://nph.onlinelibrary.wiley.com/doi/10.1111/nph.16937 This article may be used for non-commercial purposes in accordance With Wiley Terms and Conditions for self-archiving.
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Available under license: CC BY-NC: Creative Commons Attribution-NonCommercial 4.0 International License
Final published version
Licence: CC BY: Creative Commons Attribution 4.0 International License
Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - Heat-induced changes in the abundance of wheat Rubisco activase isoforms
AU - Degen, Gustaf E.
AU - Orr, Douglas
AU - Carmo-Silva, Elizabete
PY - 2021/2/1
Y1 - 2021/2/1
N2 - The Triticum aestivum (wheat) genome encodes three isoforms of Rubisco activase (Rca) differing in thermostability, which could be exploited to improve the resilience of this crop to global warming. We hypothesized that elevated temperatures would cause an increase in the relative abundance of heat‐stable Rca1β.Wheat plants were grown at 25° C : 18°C (day : night) and exposed to heat stress (38° C : 22°C) for up to 5 d at pre‐anthesis. Carbon (C) assimilation, Rubisco activity, CA1Pase activity, transcripts of Rca1β, Rca2β, and Rca2α, and the quantities of the corresponding protein products were measured during and after heat stress.The transcript of Rca1β increased 40‐fold in 4 h at elevated temperatures and returned to the original level after 4 h upon return of plants to control temperatures. Rca1β comprised up to 2% of the total Rca protein in unstressed leaves but increased three‐fold in leaves exposed to elevated temperatures for 5 d and remained high at 4 h after heat stress.These results show that elevated temperatures cause rapid changes in Rca gene expression and adaptive changes in Rca isoform abundance. The improved understanding of the regulation of C assimilation under heat stress will inform efforts to improve wheat productivity and climate resilience.
AB - The Triticum aestivum (wheat) genome encodes three isoforms of Rubisco activase (Rca) differing in thermostability, which could be exploited to improve the resilience of this crop to global warming. We hypothesized that elevated temperatures would cause an increase in the relative abundance of heat‐stable Rca1β.Wheat plants were grown at 25° C : 18°C (day : night) and exposed to heat stress (38° C : 22°C) for up to 5 d at pre‐anthesis. Carbon (C) assimilation, Rubisco activity, CA1Pase activity, transcripts of Rca1β, Rca2β, and Rca2α, and the quantities of the corresponding protein products were measured during and after heat stress.The transcript of Rca1β increased 40‐fold in 4 h at elevated temperatures and returned to the original level after 4 h upon return of plants to control temperatures. Rca1β comprised up to 2% of the total Rca protein in unstressed leaves but increased three‐fold in leaves exposed to elevated temperatures for 5 d and remained high at 4 h after heat stress.These results show that elevated temperatures cause rapid changes in Rca gene expression and adaptive changes in Rca isoform abundance. The improved understanding of the regulation of C assimilation under heat stress will inform efforts to improve wheat productivity and climate resilience.
U2 - 10.1111/nph.16937
DO - 10.1111/nph.16937
M3 - Journal article
VL - 229
SP - 1298
EP - 1311
JO - New Phytologist
JF - New Phytologist
SN - 0028-646X
IS - 3
ER -