用户名: 密码: 验证码:
Temperature responses of the Rubisco maximum carboxylase activity across domains of life: phylogenetic signals, trade-offs, and importance for carbon gain
详细信息    查看全文
  • 作者:J. Galmés ; M. V. Kapralov ; L. O. Copolovici ; C. Hermida-Carrera…
  • 关键词:Activation energy ; Adaptation ; Carboxylation ; Evolution ; Photosynthesis ; Temperature dependencies
  • 刊名:Photosynthesis Research
  • 出版年:2015
  • 出版时间:February 2015
  • 年:2015
  • 卷:123
  • 期:2
  • 页码:183-201
  • 全文大小:607 KB
  • 参考文献:1. Ackerly DD, Reich PB (1999) Convergence and correlations among leaf size and function in seed plants: a comparative test using independent contrasts. Am J Bot 86:1272-281
    2. Ainsworth EA, Ort DR (2010) How do we improve crop production in a warming world? Plant Physiol 154:526-30
    3. An SJ, Pandeya D, Park SW, Li J, Kwon JK, Koeda S, Hosokawa M, Paek NC, Choi D, Kang BC (2011) Characterization and genetic analysis of a low-temperature-sensitive mutant, sy-2, in / Capsicum chinense. Theor Appl Genet 122:459-70
    4. Archontoulis SV, Yin X, Vos J, Danalatos NG, Struik PC (2012) Leaf photosynthesis and respiration of three bioenergy crops in relation to temperature and leaf nitrogen: how conserved are biochemical model parameters among crop species? J Exp Bot 63:895-11
    5. Badger MR (1980) Kinetic properties of ribulose 1,5-bisphosphate carboxylase/oxygenase from / Anabaena variabilis. Arch Biochem Biophys 201:247-54
    6. Badger MR, Andrews TJ (1974) Effects of CO2, O2 and temperature on a high-affinity form of ribulose diphosphate carboxylase/oxygenase from spinach. Biochem Biophys Res Commun 60:204-10
    7. Badger MR, Andrews TJ (1987) Co-evolution of Rubisco and CO2 concentrating mechanisms. In: Biggens J (ed) Progress in photosynthesis research. Martinus Nijhoff Publishers, Dordrecht, pp 601-09
    8. Badger MR, Collatz GJ (1977) Studies on the kinetic mechanism of ribulose-1,5-bisphosphate carboxylase and oxygenase reactions, with particular reference to the effect of temperature on kinetic parameters. Carnegie Inst Wash Year b 76:355-61
    9. Bermúdez MA, Galmés J, Moreno I, Mullineaux PM, Gotor C, Romero LC (2012) Photosynthetic adaptation to length of day is dependent on S-sulfocysteine synthase activity in the thylakoid lumen. Plant Physiol 160:274-88
    10. Bernacchi CJ, Singsaas EL, Pimentel C, Portis AR, Long SP (2001) Improved temperature response functions for models of Rubisco-limited photosynthesis. Plant Cell Environ 24:253-59
    11. Bernacchi CJ, Pimentel C, Long SP (2003) / In vivo temperature response functions of parameters required to model RuBP-limited photosynthesis. Plant Cell Environ 26:1419-430
    12. Berry J, Bj?rkman O (1980) Photosynthetic response and adaptation to temperature in higher plants. Annu Rev Plant Physiol 31:491-43
    13. Bilger W, Schreiber U U, Lange OL (1987) Chlorophyll fluorescence as an indicator of heat induced limitation of photosynthesis in / Arbutus unedo L. In: Tenhunen JD, Catarino FM, Lange OL, Oechel WC (eds) Plant response to stress. Functional analysis in Mediterranean ecosystems, NATO ASI series, series G: ecological sciences, vol 15. Springer, Berlin, pp 391-99
    14. Bj?rkman O, Badger MR, Armond PA (1980) Response and adaptation of photosynthesis to high temperatures. In: Turner NC, Kramer PJ (eds) Adaptation of plants to water and high temperature stress. Wiley, New York, pp 233-49
    15. Blomberg SP, Garland T (2002) Tempo and mode in evolution: phylogenetic inertia, adaptation and comparative methods. J Evol Biol 15:899-10
    16. Bowes G, Ogren WL, Hageman RH (1972) Light saturation, photosynthesis rate, RuDP carboxylase activity, and specific leaf weight in soybeans grown under different light intensities. Crop Sci 12:77-9
    17. Bracher A, Starling-Windhof A, Hartl FU, Hayer-Hartl M (2011) Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco. Nat Struct Mol Biol 18:875-80
    18. Breen MS, Kemena C, Vlasov PK, Notredame C, Kondrashov FA (2012) Epistasis as the primary factor in molecular evolution. Nature 490:535-38
    19. Brooks A, Farquhar GD (1985) Effect of temperature on the CO2/O2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase and the rate of respiration in the light. Planta 165:397-06
    20. Bunce JA (2000) Acclimation of photosynthesis to temperature in eight cool and warm climate herbaceous C3 species: temperature dependence of parameters of a biochemical photosynthesis model. Photosynth Res 63:59-7
    21. Castrillo M (1995) Ribulose-1,5-bis-phosphate carboxylase activity in altitudinal populations of / Espeletia schultzii Wedd. Oecologia 101:193-96
    22. Cavanagh AP, Kubien DS (2013) Can phenotypic plasticity in Rubisco performance contribute to photosynthetic acclimation? Photosynth Res 119:203-14
    23. Cen YP, Sage RF (2005) The regulation of Rubisco activity in response to variation in temperature and atmospheric CO2 partial pressure in sweet potato. Plant Physiol 139:979-90
    24. Chabot BF, Chabot JF, Billings WD (1972) Ribulose-1,5-diphosphate carboxylase activity in arctic and alpine populations of / Oxyria digyna. Photosynthetica 6:364-69
    25. Christin PA, Salamin N, Muasya AM, Roalson EH
  • 作者单位:J. Galmés (1)
    M. V. Kapralov (2)
    L. O. Copolovici (3)
    C. Hermida-Carrera (1)
    ü. Niinemets (3) (4)

    1. Research Group in Plant Biology Under Mediterranean Conditions, Department of Biology, Universitat de les Illes Balears, Carretera de Valldemossa km 7.5, 07122, Palma, Illes Balears, Spain
    2. Plant Science Division, Research School of Biology, The Australian National University, Acton, Canberra, ACT, 2601, Australia
    3. Institute of Agricultural and Environmental Sciences, Estonian University of Life Sciences, Kreutzwaldi 1, 51014, Tartu, Estonia
    4. Estonian Academy of Sciences, Kohtu 6, 10130, Tallinn, Estonia
  • 刊物类别:Biomedical and Life Sciences
  • 刊物主题:Life Sciences
    Plant Physiology
  • 出版者:Springer Netherlands
  • ISSN:1573-5079
文摘
Temperature response of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalytic properties directly determines the CO2 assimilation capacity of photosynthetic organisms as well as their survival in environments with different thermal conditions. Despite unquestionable importance of Rubisco, the comprehensive analysis summarizing temperature responses of Rubisco traits across lineages of carbon-fixing organisms is lacking. Here, we present a review of the temperature responses of Rubisco carboxylase specific activity ( \(k_{\text{cat}}^{\text{c}}\) ) within and across domains of life. In particular, we consider the variability of temperature responses, and their ecological, physiological, and evolutionary controls. We observed over two-fold differences in the energy of activation (ΔH a) among different groups of photosynthetic organisms, and found significant differences between C3 plants from cool habitats, C3 plants from warm habitats and C4 plants. According to phylogenetically independent contrast analysis, ΔH a was not related to the species optimum growth temperature (T growth), but was positively correlated with Rubisco specificity factor (S c/o) across all organisms. However, when only land plants were analyzed, ΔH a was positively correlated with both T growth and S c/o, indicating different trends for these traits in plants versus unicellular aquatic organisms, such as algae and bacteria. The optimum temperature (T opt) for \(k_{\text{cat}}^{\text{c}}\) correlated with S c/o for land plants and for all organisms pooled, but the effect of T growth on T opt was driven by species phylogeny. The overall phylogenetic signal was significant for all analyzed parameters, stressing the importance of considering the evolutionary framework and accounting for shared ancestry when deciphering relationships between Rubisco kinetic parameters. We argue that these findings have important implications for improving global photosynthesis models.

© 2004-2018 中国地质图书馆版权所有 京ICP备05064691号 京公网安备11010802017129号

地址:北京市海淀区学院路29号 邮编:100083

电话:办公室:(+86 10)66554848;文献借阅、咨询服务、科技查新:66554700