Abstract
The acclimation of higher plants to different light intensities is associated with a reorganization of the photosynthetic apparatus. These modifications, namely, changes in the amount of peripheral antenna (LHCII) of photosystem (PS) II and changes in PSII/PSI stoichiometry, typically lead to an altered chlorophyll (Chl) a/b ratio. However, our previous studies show that in spruce, this ratio is not affected by changes in growth light intensity. The evolutionary loss of PSII antenna proteins LHCB3 and LHCB6 in the Pinaceae family is another indication that the light acclimation strategy in spruce could be different. Here we show that, unlike Arabidopsis, spruce does not modify its PSII/PSI ratio and PSII antenna size to maximize its photosynthetic performance during light acclimation. Its large PSII antenna consists of many weakly bound LHCIIs, which form effective quenching centers, even at relatively low light. This, together with sensitive photosynthetic control on the level of cytochrome b6f complex (protecting PSI), is the crucial photoprotective mechanism in spruce. High-light acclimation of spruce involves the disruption of PSII macro-organization, reduction of the amount of both PSII and PSI core complexes, synthesis of stress proteins that bind released Chls, and formation of “locked-in” quenching centers from uncoupled LHCIIs. Such response has been previously observed in the evergreen angiosperm Monstera deliciosa exposed to high light. We suggest that, in contrast to annuals, shade-tolerant evergreen land plants have their own strategy to cope with light intensity changes and the hallmark of this strategy is a stable Chl a/b ratio.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Data availability
All relevant data can be found within the manuscript and its supporting materials. Mass spectrometry proteomics data were deposited to the ProteomeXchange Consortium via PRIDE partner repository under dataset identifier PXD029868.
References
Adamska I, Kruse E, Kloppstech K (2001) Stable insertion of the early light-induced proteins into etioplast membranes requires chlorophyll a. J Biol Chem 276:8582–8587. https://doi.org/10.1074/jbc.M010447200
Albanese P, Manfredi M, Meneghesso A, Marengo E, Saracco G, Barber J, Morosinotto T, Pagliano C (2016) Dynamic reorganization of photosystem II supercomplexes in response to variations in light intensities. Biochim Biophys Acta Bioenerg 1857:1651–1660. https://doi.org/10.1016/j.bbabio.2016.06.011
Albanese P, Manfredi M, Re A, Marengo E, Saracco G, Pagliano C (2018) Thylakoid proteome modulation in pea plants grown at different irradiances: quantitative proteomic profiling in a non-model organism aided by transcriptomic data integration. Plant J 96:786–800. https://doi.org/10.1111/tpj.14068
Albanese P, Manfredi M, Marengo E, Saracco G, Pagliano C (2019) Structural and functional differentiation of the light-harvesting protein Lhcb4 during land plant diversification. Physiol Plant 166:336–350. https://doi.org/10.1111/ppl.12964
Allen JF (2017) Why we need to know the structure of phosphorylated chloroplast light-harvesting complex II. Physiol Plant 161:28–44. https://doi.org/10.1111/ppl.12577
Anderson JM (1986) Photoregulation of the composition, function, and structure of thylakoid membranes. Annu Rev Plant Physiol Plant Mol Biol 37:93–136. https://doi.org/10.1146/annurev.arplant.37.1.93
Anderson JM, Chow WS, Goodchild DJ (1988) Thylakoid membrane organization in sun/shade acclimation. Aust J Plant Physiol 15:11–26. https://doi.org/10.1071/PP9880011
Bag P, Chukhutsina V, Zhang ZS, Paul S, Ivanov AG, Shutova T, Croce R, Holzwarth AR, Jansson S (2020) Direct energy transfer from photosystem II to photosystem I confers winter sustainability in Scots Pine. Nat Commun 11:6388. https://doi.org/10.1038/s41467-020-20137-9
Bai TY, Guo L, Xu MY, Tian LR (2021) Structural diversity of Photosystem I and its light-harvesting system in eukaryotic algae and plants. Front Plant Sci 12:781035. https://doi.org/10.3389/fpls.2021.781035
Bailey S, Walters RG, Jansson S, Horton P (2001) Acclimation of Arabidopsis thaliana to the light environment: the existence of separate low light and high light responses. Planta 213:794–801. https://doi.org/10.1007/s004250100556
Baker NR (2008) Chlorophyll fluorescence: a probe of photosynthesis in vivo. Annu Rev Plant Biol 59:89–113. https://doi.org/10.1146/annurev.arplant.59.032607.092759
Ballottari M, Dall’Osto L, Morosinotto T, Bassi R (2007) Contrasting behavior of higher plant photosystem I and II antenna systems during acclimation. J Biol Chem 282:8947–8958. https://doi.org/10.1074/jbc.M606417200
Barzda V, Mustardy L, Garab G (1994) Size dependency of circular-dichroism in macroaggregates of photosynthetic pigment-protein complexes. Biochemistry 33:10837–10841. https://doi.org/10.1021/bi00201a034
Bassi R, Dall’Osto L (2021) Dissipation of light energy absorbed in excess: the molecular mechanisms. Annu Rev Plant Biol 72:47–76. https://doi.org/10.1146/annurev-arplant-071720-015522
Belgio E, Johnson MP, Juric S, Ruban AV (2012) Higher plant photosystem II light-harvesting antenna, not the reaction center, determines the excited-state lifetime-both the maximum and the nonphotochemically quenched. Biophys J 102:2761–2771. https://doi.org/10.1016/j.bpj.2012.05.004
Belgio E, Trsková E, Kotabová E, Ewe D, Prášil O, Kaňa R (2018) High light acclimation of Chromera velia points to photoprotective NPQ. Photosynth Res 135:263–274. https://doi.org/10.1007/s11120-017-0385-8
Bielczynski LW, Schansker G, Croce R (2016) Effect of light acclimation on the organization of photosystem II super- and sub-complexes in Arabidopsis thaliana. Front Plant Sci 7:105. https://doi.org/10.3389/fpls.2016.00105
Bilger W, Björkman O (1990) Role of the xanthophyll cycle in photoprotection elucidated by measurements of light-induced absorbance changes, fluorescence and photosynthesis in leaves of Hedera canariensis. Photosynth Res 25:173–185. https://doi.org/10.1007/BF00033159
Björkman O, Demmig B (1987) Photon yield of O2 evolution and chlorophyll fluorescence characteristics at 77 K among vascular plants of diverse origins. Planta 170:489–504. https://doi.org/10.1007/BF00402983
Bukhov NG, Carpentier R (2003) Measurement of photochemical quenching of absorbed quanta in photosystem I of intact leaves using simultaneous measurements of absorbance changes at 830 nm and thermal dissipation. Planta 216:630–638. https://doi.org/10.1007/s00425-002-0886-2
Caffarri S, Kouřil R, Kereiche S, Boekema EJ, Croce R (2009) Functional architecture of higher plant photosystem II supercomplexes. EMBO J 28:3052–3063. https://doi.org/10.1038/emboj.2009.232
Chmeliov J, Gelzinis A, Songaila E, Augulis R, Duffy CDP, Ruban AV, Valkunas L (2016) The nature of self-regulation in photosynthetic light-harvesting antenna. Nat Plants 2:16045. https://doi.org/10.1038/NPLANTS.2016.45
Chukhutsina VU, Liu X, Xu P, Croce R (2020) Light-harvesting complex II is an antenna of photosystem I in dark-adapted plants. Nat Plants 6:860–868. https://doi.org/10.1038/s41477-020-0693-4
Croce R (2020) Beyond ‘seeing is believing’: the antenna size of the photosystems in vivo. New Phytol 228:1214–1218. https://doi.org/10.1111/nph.16758
Dainese P, Bassi R (1991) Subunit stoichiometry of the chloroplast photosystem II antenna system and aggregation state of the component chlorophyll a/b binding proteins. J Biol Chem 266:8136–8142. https://doi.org/10.1016/S0021-9258(18)92952-2
Dau H, Andrews JC, Roelofs TA, Latimer MJ, Liang WC, Yachandra VK, Sauer K, Klein MP (1995) Structural consequences of ammonia binding to the manganese center of the photosynthetic oxygen-evolving complex: an X-ray absorption spectroscopy study of isotropic and oriented photosystem II particles. Biochemistry 34:5274–5287. https://doi.org/10.1021/bi00015a043
de Bianchi S, Ballottari M, Dall’Osto L, Bassi R (2010) Regulation of plant light harvesting by thermal dissipation of excess energy. Biochem Soc Trans 38:651–660. https://doi.org/10.1042/BST0380651
Dekker JP, Boekema EJ (2005) Supramolecular organization of thylakoid membrane proteins in green plants. Biochim Biophys Acta Bioenerg 1706:12–39. https://doi.org/10.1016/j.bbabio.2004.09.009
Demmig-Adams B, Adams WW (2006) Photoprotection in an ecological context: the remarkable complexity of thermal energy dissipation. New Phytol 172:11–21. https://doi.org/10.1111/j.1469-8137.2006.01835.x
Demmig-Adams B, Ebbert V, Mellman DL, Mueh KE, Schaffer L, Funk C, Zarter CR, Adamska I, Jansson S, Adams WW III (2006) Modulation of PsbS and flexible vs sustained energy dissipation by light environment in different species. Physiol Plant 127:670–680. https://doi.org/10.1111/j.1399-3054.2006.00698.x
Demmig-Adams B, Cohu CM, Muller O, Adams WW III (2012) Modulation of photosynthetic energy conversion efficiency in nature: from seconds to seasons. Photosynth Res 113:75–88. https://doi.org/10.1007/s11120-012-9761-6
Demmig-Adams B, Koh SC, Cohu CM, Muller O, Stewart JJ, Adams WW III (2014) Non-photochemical fluorescence quenching in contrasting plant species and environments. In: Demmig-Adams B, Garab G, Adams WW III, Govindjee (eds) Non-photochemical quenching and energy dissipation in plants, algae and cyanobacteria. Advances in photosynthesis and respiration 40. Springer, Dordrecht, pp 531–552
Dlouhý O, Karlický V, Arshad R, Zsiros O, Domonkos I, Kurasová I, Wacha AF, Morosinotto T, Bóta A, Kouřil R, Špunda V, Garab G (2021) Lipid polymorphism of the subchloroplast-granum and stroma thylakoid membrane-particles. II Structure and functions. Cells 10:2363. https://doi.org/10.3390/cells10092363
Dobrikova AG, Varkonyi Z, Krumova SB, Kovacs L, Kostov GK, Todinova SJ, Busheva MC, Taneva SG, Garab G (2003) Structural rearrangements in chloroplast thylakoid membranes revealed by differential scanning calorimetry and circular dichroism spectroscopy. Thermo-optic effect. Biochemistry 42:11272–11280. https://doi.org/10.1021/bi034899j
Eberhard S, Finazzi G, Wollman FA (2008) The dynamics of photosynthesis. Annu Rev Genet 42:463–515. https://doi.org/10.1146/annurev.genet.42.110807.091452
Ferroni L, Suorsa M, Aro EM, Baldisserotto C, Pancaldi S (2016) Light acclimation in the lycophyte Selaginella martensii depends on changes in the amount of photosystems and on the flexibility of the light-harvesting complex II antenna association with both photosystems. New Phytol 211:554–568. https://doi.org/10.1111/nph.13939
Floris M, Bassi R, Robaglia C, Alboresi A, Lanet E (2013) Post-transcriptional control of light-harvesting genes expression under light stress. Plant Mol Biol 82:147–154. https://doi.org/10.1007/s11103-013-0046-z
Garab G, Kieleczawa J, Sutherland JC, Bustamante C, Hind G (1991) Organization of pigment protein complexes into macrodomains in the thylakoid membranes of wild-type and chlorophyll b-less mutant of barley as revealed by circular dichroism. Photochem Photobiol 54:273–281. https://doi.org/10.1111/j.1751-1097.1991.tb02016.x
Genty B, Briantais JM, Baker NR (1989) The relationship between the quantum yield of photosynthetic electron transport and quenching of chlorophyll fluorescence. Biochim Biophys Acta 990:87–92. https://doi.org/10.1016/S0304-4165(89)80016-9
Gerotto C, Alboresi A, Giacometti GM, Bassi R, Morosinotto T (2011) Role of PSBS and LHCSR in Physcomitrella patens acclimation to high light and low temperature. Plant Cell Environ 34:922–932. https://doi.org/10.1111/j.1365-3040.2011.02294.x
Gilmore AM, Yamamoto HY (1991) Zeaxanthin formation and energy-dependent fluorescence quenching in pea chloroplasts under artificially mediated linear and cyclic electron transport. Plant Physiol 96:635–643. https://doi.org/10.1104/pp.96.2.635
Grebe S, Trotta A, Bajwa AA, Suorsa M, Gollan PJ, Jansson S, Tikkanen M, Aro EM (2019) The unique photosynthetic apparatus of Pinaceae: analysis of photosynthetic complexes in Picea abies. J Exp Bot 70:3211–3225. https://doi.org/10.1093/jxb/erz127
Grebe S, Trotta A, Bajwa AA, Mancini I, Bag P, Jansson S, Tikkanen M, Aro EM (2020) Specific thylakoid protein phosphorylations are prerequisites for overwintering of Norway spruce (Picea abies) photosynthesis. Proc Natl Acad Sci USA 117:17499–17509. https://doi.org/10.1073/pnas.2004165117
Hutin C, Nussaume L, Moise N, Moya I, Kloppstech K, Havaux M (2003) Early light-induced proteins protect Arabidopsis from photooxidative stress. Proc Natl Acad Sci USA 100:4921–4926. https://doi.org/10.1073/pnas.0736939100
Ilík P, Pavlovič A, Kouřil R, Alboresi A, Morosinotto T, Allahverdiyeva Y, Aro EM, Yamamoto H, Shikanai T (2017) Alternative electron transport mediated by flavodiiron proteins is operational in organisms from cyanobacteria up to gymnosperms. New Phytol 214:967–972. https://doi.org/10.1111/nph.14536
Ilíková I, Ilík P, Opatíková M, Arshad R, Nosek L, Karlický V, Kučerová Z, Roudnický P, Pospíšil P, Lazár D, Bartoš J, Kouřil R (2021) Towards spruce-type photosystem II: consequences of the loss of light-harvesting proteins LHCB3 and LHCB6 in Arabidopsis. Plant Physiol 187:2691–2715. https://doi.org/10.1093/plphys/kiab396
Jajoo A, Mekala NR, Tongra T, Tiwari A, Grieco M, Tikkanen M, Aro EM (2014) Low pH-induced regulation of excitation energy between the two photosystems. FEBS Lett 588:970–974. https://doi.org/10.1016/j.febslet.2014.01.056
Karlický V, Kurasová I, Ptáčková B, Večeřová K, Urban O, Špunda V (2016) Enhanced thermal stability of the thylakoid membranes from spruce. A comparison with selected angiosperms. Photosynth Res 130:357–371. https://doi.org/10.1007/s11120-016-0269-3
Karlický V, Kmecová Materová Z, Kurasová I, Nezval J, Štroch M, Garab G, Špunda V (2021) Accumulation of geranylgeranylated chlorophylls in the pigment-protein complexes of Arabidopsis thaliana acclimated to green light: effects on the organization of light-harvesting complex II and photosystem II functions. Photosynth Res 149:233–252. https://doi.org/10.1007/s11120-021-00827-1
Kirchhoff H (2013) Architectural switches in plant thylakoid membranes. Photosynth Res 116:481–487. https://doi.org/10.1007/s11120-013-9843-0
Klughammer C, Schreiber U (2008) Saturation pulse method for assessment of energy conversion in PSI. PAM Appl Notes 1:11–14
Kouřil R, Dekker JP, Boekema EJ (2012) Supramolecular organization of photosystem II in green plants. Biochim Biophys Acta Bioenerg 1817:2–12. https://doi.org/10.1016/j.bbabio.2011.05.024
Kouřil R, Wientjes E, Bultema JB, Croce R, Boekema EJ (2013) High-light vs. low-light: Effect of light acclimation on photosystem II composition and organization in Arabidopsis thaliana. Biochim Biophys Acta Bioenerg 1827:411–419. https://doi.org/10.1016/j.bbabio.2012.12.003
Kouřil R, Nosek L, Bartoš J, Boekema EJ, Ilík P (2016) Evolutionary loss of light-harvesting proteins Lhcb6 and Lhcb3 in major land plant groups - break-up of current dogma. New Phytol 210:808–814. https://doi.org/10.1111/nph.13947
Kouřil R, Nosek L, Semchonok D, Boekema EJ, Ilík P (2018) Organization of plant photosystem II and photosystem I supercomplexes. Subcell Biochem 87:259–286. https://doi.org/10.1007/978-981-10-7757-9_9
Kouřil R, Nosek L, Opatíková M, Arshad R, Semchonok DA, Chamrád I, Lenobel R, Boekema EJ, Ilík P (2020) Unique organization of photosystem II supercomplexes and megacomplexes in Norway spruce. Plant J 104:215–225. https://doi.org/10.1111/tpj.14918
Kovács L, Damkjӕr J, Kereïche S, Ilioaia C, Ruban AV, Boekema EJ, Jansson S, Horton P (2006) Lack of the light-harvesting complex CP24 affects the structure and function of the grana membranes of higher plant chloroplasts. Plant Cell 18:3106–3120. https://doi.org/10.1105/tpc.106.045641
Kramer DM, Johnson G, Kiirats O, Edwards GE (2004) New fluorescence parameters for the determination of QA redox state and excitation energy fluxes. Photosynth Res 79:209–218. https://doi.org/10.1023/B:PRES.0000015391.99477.0d
Kurasová I, Kalina J, Urban O, Štroch M, Špunda V (2003) Acclimation of two distinct plant species, spring barley and Norway spruce, to combined effect of various irradiance and CO2 concentration during cultivation in controlled environment. Photosynthetica 41:513–523. https://doi.org/10.1023/B:PHOT.0000027515.05641.fd
Li YH, Liu B, Zhang J, Kong FN, Zhang L, Meng H, Li WJ, Rochaix JD, Li D, Peng LW (2019) OHP1, OHP2, and HCF244 form a transient functional complex with the Photosystem II reaction center. Plant Physiol 179:195–208. https://doi.org/10.1104/pp.18.01231
Lichtenthaler HK (1987) Chlorophylls and carotenoids: pigments of photosynthetic biomembranes. In: Douce R, Packer L (eds) Methods in enzymology. Academic Press Inc., New York, pp 350–382
Michael TP, Bryant D, Gutierrez R, Borisjuk N, Chu P, Zhang HZ, Xia J, Zhou JF, Peng H, El Baidouri M et al (2017) Comprehensive definition of genome features in Spirodela polyrhiza by high-depth physical mapping and short-read DNA sequencing strategies. Plant J 89:617–635. https://doi.org/10.1111/tpj.13400
Miloslavina Y, Wehner A, Lambrev PH, Wientjes E, Reus M, Garab G, Croce R, Holzwarth AR (2008) Far-red fluorescence: a direct spectroscopic marker for LHCII oligomer formation in non-photochemical quenching. FEBS Lett 582:3625–3631. https://doi.org/10.1016/j.febslet.2008.09.044
Miyake C, Miyata M, Shinzaki Y, Tomizawa K (2005) CO2 response of cyclic electron flow around PSI (CEF-PSI) in tobacco leaves—relative electron fluxes through PSI and PSII determine the magnitude of non-photochemical quenching (NPQ) of Chl fluorescence. Plant Cell Physiol 46:629–637. https://doi.org/10.1093/pcp/pci067
Murchie EH, Horton P (1997) Acclimation of photosynthesis to irradiance and spectral quality in British plant species: chlorophyll content, photosynthetic capacity and habitat preference. Plant Cell Environ 20:438–448. https://doi.org/10.1046/j.1365-3040.1997.d01-95.x
Nama S, Madireddi SK, Yadav RM, Subramanyam R (2019) Non-photochemical quenching-dependent acclimation and thylakoid organization of Chlamydomonas reinhardtii to high light stress. Photosynth Res 139:387–400. https://doi.org/10.1007/s11120-018-0551-7
Ostroumov EE, Gotze JP, Reus M, Lambrev PH, Holzwarth AR (2020) Characterization of fluorescent chlorophyll charge-transfer states as intermediates in the excited state quenching of light-harvesting complex II. Photosynth Res 144:171–193. https://doi.org/10.1007/s11120-020-00745-8
Rochaix JD, Bassi R (2019) LHC-like proteins involved in stress responses and biogenesis/repair of the photosynthetic apparatus. Biochem J 476:581–593. https://doi.org/10.1042/BCJ20180718
Rott M, Martins NF, Thiele W, Lein W, Bock R, Kramer DM, Schöttler MA (2011) ATP synthase repression in tobacco restricts photosynthetic electron transport, CO2 assimilation, and plant growth by overacidification of the thylakoid lumen. Plant Cell 23:304–321. https://doi.org/10.1105/tpc.110.079111
Ruban AV, Wilson S (2021) The mechanism of non-photochemical quenching in plants: localization and driving forces. Plant Cell Physiol 62:1063–1072. https://doi.org/10.1093/pcp/pcaa155
Schöttler MA, Tóth SZ (2014) Photosynthetic complex stoichiometry dynamics in higher plants: environmental acclimation and photosynthetic flux control. Front Plant Sci 5:188. https://doi.org/10.3389/fpls.2014.00188
Shen LL, Huang ZH, Chang SH, Wang WD, Wang JF, Kuang TY, Han GY, Shen JR, Zhang X (2019) Structure of a C2S2M2N2 type PSII-LHCII supercomplex from the green alga Chlamydomonas reinhardtii. Proc Natl Acad Sci USA 116:21246–21255. https://doi.org/10.1073/pnas.1912462116
Sheng X, Watanabe A, Li AJ, Kim E, Song CH, Murata K, Song DF, Minagawa J, Liu ZF (2019) Structural insight into light harvesting for photosystem II in green algae. Nat Plants 5:1320–1330. https://doi.org/10.1038/s41477-019-0543-4
Štroch M, Kuldová K, Kalina J, Špunda V (2008) Dynamics of the xanthophyll cycle and non-radiative dissipation of absorbed light energy during exposure of Norway spruce to high irradiance. J Plant Physiol 165:612–622. https://doi.org/10.1016/j.jplph.2007.03.013
Su XD, Ma J, Wei XP, Cao P, Zhu DJ, Chang WR, Liu ZF, Zhang XZ, Li M (2017) Structure and assembly mechanism of plant C2S2M2-type PSII-LHCII supercomplex. Science 357:815–520. https://doi.org/10.1126/science.aan0327
Tikhonov AN (2013) pH-dependent regulation of electron transport and ATP synthesis in chloroplasts. Photosynth Res 116:511–534. https://doi.org/10.1007/s11120-013-9845-y
Tikkanen M, Nurmi M, Kangasjärvi S, Aro EM (2008) Core protein phosphorylation facilitates the repair of photodamaged photosystem II at high light. Biochim Biophys Acta Bioenerg 1777:1432–1437. https://doi.org/10.1016/j.bbabio.2008.08.004
Tóth TN, Rai N, Solymosi K, Zsiros O, Schröder WP, Garab G, van Amerongen H, Horton P, Kovács L (2016) Fingerprinting the macro-organisation of pigment-protein complexes in plant thylakoid membranes in vivo by circular-dichroism spectroscopy. Biochim Biophys Acta Bioenerg 1857:1479–1489. https://doi.org/10.1016/j.bbabio.2016.04.287
van Bezouwen LS, Caffarri S, Kale RS, Kouřil R, Thunnissen A, Oostergetel GT, Boekema EJ (2017) Subunit and chlorophyll organization of the plant photosystem II supercomplex. Nat Plants 3:17080. https://doi.org/10.1038/nplants.2017.80
Van Grondelle R, Dekker JP, Gillbro T, Sundstrom V (1994) Energy-transfer and trapping in photosynthesis. Biochim Biophys Acta Bioenerg 1187:1–65. https://doi.org/10.1016/0005-2728(94)90166-X
Walters RG (2005) Towards an understanding of photosynthetic acclimation. J Exp Bot 56:435–447. https://doi.org/10.1093/jxb/eri060
Ware MA, Belgio E, Ruban AV (2015) Photoprotective capacity of non-photochemical quenching in plants acclimated to different light intensities. Photosynth Res 126:261–274. https://doi.org/10.1007/s11120-015-0102-4
Weis E (1985) Chlorophyll fluorescence at 77 K in intact leaves—characterization of a technique to eliminate artifacts related to self-absorption. Photosynth Res 6:73–86. https://doi.org/10.1007/BF00029047
Wientjes E, van Amerongen H, Croce R (2013a) LHCII is an antenna of both photosystems after long-term acclimation. Biochim Biophys Acta Bioenerg 1827:420–426. https://doi.org/10.1016/j.bbabio.2012.12.009
Wientjes E, van Amerongen H, Croce R (2013b) Quantum yield of charge separation in photosystem II: functional effect of changes in the antenna size upon light acclimation. J Phys Chem B 117:11200–11208. https://doi.org/10.1021/jp401663w
Wiśniewski JR, Zougman A, Nagaraj N, Mann M (2009) Universal sample preparation method for proteome analysis. Nat Methods 6:359–362. https://doi.org/10.1038/NMETH.1322
Yamamoto H, Shikanai T (2019) PGR5-dependent cyclic electron flow protects photosystem I under fluctuating light at donor and acceptor sides. Plant Physiol 179:588–600. https://doi.org/10.1104/pp.18.01343
Yamamoto H, Takahashi S, Badger MR, Shikanai T (2016) Artificial remodelling of alternative electron flow by flavodiiron proteins in Arabidopsis. Nat Plants 2:16012. https://doi.org/10.1038/NPLANTS.2016.12
Acknowledgements
This work was supported by the Grant Agency of the Czech Republic (Projects No. 18-12178S and 21-05497S) and the European Regional Development Fund (ERDF) Projects “Plants as a tool for sustainable global development” (no. CZ.02.1.01/0.0/0.0/16_019/0000827) and “SustES—Adaptation strategies for sustainable ecosystem services and food security under adverse environmental conditions” (CZ.02.1.01/0.0/0.0/16_019/0000797). CIISB, Instruct-CZ Centre of Instruct-ERIC EU consortium, funded by MEYS CR infrastructure Project LM2018127, is gratefully acknowledged for the financial support of the measurements at the CEITEC Proteomics Core Facility. The authors thank prof. Toshiharu Shikanai for providing us with seeds of transgenic Arabidopsis thaliana expressing flavodiiron genes flvA and flvB from the moss Physcomitrella patens, Běla Piskořová for technical assistance, and Lena Hunt for language editing of the manuscript.
Author information
Authors and Affiliations
Contributions
RK, MŠ, VK, VŠ, and PI planned and designed the research; all the authors performed experiments and/or analyzed the data. MŠ, VK, PI, II, and RK wrote the manuscript with input from all the authors, and all the authors revised and approved it.
Corresponding author
Ethics declarations
Conflict of interest
The authors declare that there is no conflict of interest.
Additional information
Publisher's Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Supplementary Information
Below is the link to the electronic supplementary material.
Rights and permissions
Springer Nature or its licensor holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.
About this article
Cite this article
Štroch, M., Karlický, V., Ilík, P. et al. Spruce versus Arabidopsis: different strategies of photosynthetic acclimation to light intensity change. Photosynth Res 154, 21–40 (2022). https://doi.org/10.1007/s11120-022-00949-0
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s11120-022-00949-0