Relationship between the Heat Tolerance of Photosynthesis and the Thermal Stability of Rubisco Activase in Plants from Contrasting Thermal Environments
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Inhibition of net photosynthesis (Pn) by moderate heat stress has been attributed to an inability of Rubisco activase to maintain Rubisco in an active form. To examine this proposal, the temperature response of Pn, Rubisco activation, chlorophyll fluorescence, and the activities of Rubisco and Rubisco activase were examined in species from contrasting environments. The temperature optimum of Rubisco activation was 10 degrees C higher in the creosote bush (Larrea tridentata) compared with the Antarctic hairgrass (Deschampsia antarctica), resembling the temperature response of Pn. Pn increased markedly with increasing internal CO(2) concentration in Antarctic hairgrass and creosote bush plants subjected to moderate heat stress even under nonphotorespiratory conditions. Nonphotochemical quenching of chlorophyll fluorescence, the effective quantum yield of photochemical energy conversion (DeltaF/F(m)') and the maximum yield of PSII (F(v)/F(m)) were more sensitive to temperature in Antarctic hairgrass and two other species endemic to cold regions (i.e. Lysipomia pumila and spinach [Spinacea oleracea]) compared with creosote bush and three species (i.e. jojoba [Simmondsia chinensis], tobacco [Nicotiana tabacum], and cotton [Gossypium hirsutum]) from warm regions. The temperature response of activity and the rate of catalytic inactivation of Rubisco from creosote bush and Antarctic hairgrass were similar, whereas the optimum for ATP hydrolysis and Rubisco activation by recombinant c…
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As temperature increases above the thermal optimum to non-physiological conditions, photosynthesis may be increasingly limited due to impairment of the physical integrity of electron transport components.
“As the temperature increases further above the thermal optimum and reaches non-physiological conditions, photosynthesis may be increasingly limited due to impairment of the physical integrity of electron transport components of the photosynthetic apparatus (Salvucci and Crafts-Brandner, 2004).”
From Rubisco and Rubisco Activase Play an Important Role in the Biochemical Limitations of Photosynthesis in Rice, Wheat, and Maize under High Temperature and Water Deficit (2017) · cites this paper as Salvucci and Crafts-Brandner, 2004
The decrease in the Rubisco activation state caused a decrease in the photosynthetic capacity of the three crop species.
“Further, the decrease in the Rubisco activation state caused a decrease in the photosynthetic capacity of the three crop species (Figure 2), in agreement with previous reports (Crafts-Brandner and Salvucci, 2000; Salvucci and Crafts-Brandner, 2004; Yamori and von Caemmerer, 2009; Scafaro et al., 2012).”
From Rubisco and Rubisco Activase Play an Important Role in the Biochemical Limitations of Photosynthesis in Rice, Wheat, and Maize under High Temperature and Water Deficit (2017) · cites this paper as Salvucci and Crafts-Brandner, 2004
The results are consistent with the hypothesis that the intrinsic heat sensitivity of Rubisco activase is linked with the observed decrease in Rubisco activation.
“These results are consistent with the hypothesis that the intrinsic heat sensitivity of Rca is linked with the observed decrease in Rubisco activation (Salvucci and Crafts-Brandner, 2004; Barta et al., 2010; Carmo-Silva and Salvucci, 2011; Scafaro et al., 2016).”
From Rubisco and Rubisco Activase Play an Important Role in the Biochemical Limitations of Photosynthesis in Rice, Wheat, and Maize under High Temperature and Water Deficit (2017) · cites this paper as Salvucci and Crafts-Brandner, 2004
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References 53 · Cited by 563
- Authors
- Salvucci, M. E., & Crafts-Brandner, S. J.
- Affiliations
- Agricultural Research Service (US)
- United States Department of Agriculture, Agricultural Research Service, Western Cotton Research Laboratory, Phoenix, Arizona 85040
- Venue
- Plant Physiology
- Publisher
- Oxford University Press (OUP)
- Published
- 2004-04-01
- Volume
- 134
- Issue
- 4
- Pages
- 1460-1470
- ISSN
- 0032-0889 (ISSN-L)
- 1532-2548
- PMC
- PMC419822
- OpenAlex
- W2101552670
- Cited by
- 563
- References
- 53
- Citations by year
- 2026: 20 · 2025: 27 · 2024: 55 · 2023: 35 · 2022: 19 · 2021: 33 · 2020: 39 · 2019: 33 · 2018: 24 · 2017: 28 · 2016: 26 · 2015: 14 · 2014: 30 · 2013: 28 · 2012: 28
- FWCI
- 6.59
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model (vor)
- Locations
- PLANT PHYSIOLOGY (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Stress Responses and Tolerance
- Physical Sciences › Environmental Science › Global and Planetary Change › Plant Water Relations and Carbon Dynamics
- Keywords
- Rubisco activase, heat tolerance, photosynthesis, Rubisco activation, heat stress, thermal stability, Larrea tridentata, Deschampsia antarctica, chlorophyll fluorescence, non-photochemical quenching, photorespiration, ATP hydrolysis, endemism, optimal temperature
- MeSH terms
- Acclimatization, Adenosine Triphosphate, Carbon Dioxide, Chlorophyll, Enzyme Activation, Enzyme Stability, Hot Temperature, Molecular Sequence Data, Photosynthesis, Plant Proteins, Plants, Ribulose-Bisphosphate Carboxylase, Photosynthetic Reaction Center Complex Proteins
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