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Proc Natl Acad Sci U S A ; 117(30): 17499-17509, 2020 07 28.
Artigo em Inglês | MEDLINE | ID: mdl-32690715


Coping of evergreen conifers in boreal forests with freezing temperatures on bright winter days puts the photosynthetic machinery in great risk of oxidative damage. To survive harsh winter conditions, conifers have evolved a unique but poorly characterized photoprotection mechanism, a sustained form of nonphotochemical quenching (sustained NPQ). Here we focused on functional properties and underlying molecular mechanisms related to the development of sustained NPQ in Norway spruce (Picea abies). Data were collected during 4 consecutive years (2016 to 2019) from trees growing in sun and shade habitats. When day temperatures dropped below -4 °C, the specific N-terminally triply phosphorylated LHCB1 isoform (3p-LHCII) and phosphorylated PSBS (p-PSBS) could be detected in the thylakoid membrane. Development of sustained NPQ coincided with the highest level of 3p-LHCII and p-PSBS, occurring after prolonged coincidence of bright winter days and temperatures close to -10 °C. Artificial induction of both the sustained NPQ and recovery from naturally induced sustained NPQ provided information on differential dynamics and light-dependence of 3p-LHCII and p-PSBS accumulation as prerequisites for sustained NPQ. Data obtained collectively suggest three components related to sustained NPQ in spruce: 1) Freezing temperatures induce 3p-LHCII accumulation independently of light, which is suggested to initiate destacking of appressed thylakoid membranes due to increased electrostatic repulsion of adjacent membranes; 2) p-PSBS accumulation is both light- and temperature-dependent and closely linked to the initiation of sustained NPQ, which 3) in concert with PSII photoinhibition, is suggested to trigger sustained NPQ in spruce.

Fotossíntese , Picea/fisiologia , Estações do Ano , Proteínas das Membranas dos Tilacoides/metabolismo , Tilacoides/metabolismo , Sequência de Aminoácidos , Meio Ambiente , Complexos de Proteínas Captadores de Luz/metabolismo , Noruega , Fosforilação , Espectrometria de Massas em Tandem , Proteínas das Membranas dos Tilacoides/química , Árvores
Sci Rep ; 10(1): 6770, 2020 04 21.
Artigo em Inglês | MEDLINE | ID: mdl-32317747


Although light is essential for photosynthesis, when in excess, it may damage the photosynthetic apparatus, leading to a phenomenon known as photoinhibition. Photoinhibition was thought as a light-induced damage to photosystem II; however, it is now clear that even photosystem I may become very vulnerable to light. One main characteristic of light induced damage to photosystem II (PSII) is the increased turnover of the reaction center protein, D1: when rate of degradation exceeds the rate of synthesis, loss of PSII activity is observed. With respect to photosystem I (PSI), an excess of electrons, instead of an excess of light, may be very dangerous. Plants possess a number of mechanisms able to prevent, or limit, such damages by safe thermal dissipation of light energy (non-photochemical quenching, NPQ), slowing-down of electron transfer through the intersystem transport chain (photosynthesis-control, PSC) in co-operation with the Proton Gradient Regulation (PGR) proteins, PGR5 and PGRL1, collectively called as short-term photoprotection mechanisms, and the redistribution of light between photosystems, called state transitions (responsible of fluorescence quenching at PSII, qT), is superimposed to these short term photoprotective mechanisms. In this manuscript we have generated a number of higher order mutants by crossing genotypes carrying defects in each of the short-term photoprotection mechanisms, with the final aim to obtain a direct comparison of their role and efficiency in photoprotection. We found that mutants carrying a defect in the ΔpH-dependent photosynthesis-control are characterized by photoinhibition of both photosystems, irrespectively of whether PSBS-dependent NPQ or state transitions defects were present or not in the same individual, demonstrating the primary role of PSC in photoprotection. Moreover, mutants with a limited capability to develop a strong PSBS-dependent NPQ, were characterized by a high turnover of the D1 protein and high values of Y(NO), which might reflect energy quenching processes occurring within the PSII reaction center.

Proteínas de Arabidopsis/genética , Proteínas de Membrana/genética , Complexo de Proteínas do Centro de Reação Fotossintética/genética , Complexo de Proteína do Fotossistema I/genética , Complexo de Proteína do Fotossistema II/genética , Arabidopsis/genética , Arabidopsis/fisiologia , Genótipo , Concentração de Íons de Hidrogênio , Luz , Fotossíntese/genética , Fotossíntese/efeitos da radiação , Complexo de Proteína do Fotossistema I/efeitos da radiação , Complexo de Proteína do Fotossistema II/efeitos da radiação
Plant Physiol ; 181(4): 1615-1631, 2019 12.
Artigo em Inglês | MEDLINE | ID: mdl-31615849


Thylakoid membranes in land plant chloroplasts are organized into appressed and nonappressed membranes, which contribute to the control of energy distribution between the two photosystems (PSI and PSII) from the associated light-harvesting complexes (LHCs). Under fluctuating light conditions, fast reversible phosphorylation of the N-terminal thylakoid protein domains and changes in electrostatic forces induce modifications in thylakoid organization. To gain insight into the role and dynamics of thylakoid protein phosphorylation, we used targeted proteomics to quantify amounts of the structural proteins CURVATURE THYLAKOID1 (CURT1), including the levels of CURT1B N terminus phosphorylation and acetylation, after short-term fluctuating light treatments of Arabidopsis (Arabidopsis thaliana). The CURT1B protein was localized to a specific curvature domain separated from the margin domain, and specifically depleted of chlorophyll-binding protein complexes. The acetylation and phosphorylation of the CURT1B N terminus were mutually exclusive. The level of CURT1B phosphorylation, but not of acetylation, increased upon light shifts that also led to an increase in PSII core protein phosphorylation. These dynamics were largely absent in the knockout mutant of PSII core protein kinase SER/THR PROTEIN KINASE8 (STN8). Moreover, in mutants impaired in interaction between phosphorylated LHCII and PSI, the phosphorylation dynamics of CURT1B and the amount of the other CURT1 proteins were misregulated, indicating a functional interaction between CURT1B and PSI-LHCII complexes in grana margins. The complex relationships between phosphorylation of PSII, LHCII, and CURT1B support the dynamics of thylakoid protein complexes that are crucial in the optimization of photosynthesis under fluctuating light intensities.

Proteínas de Arabidopsis/metabolismo , Arabidopsis/metabolismo , Proteínas de Ligação a DNA/metabolismo , Complexo de Proteína do Fotossistema I/metabolismo , Tilacoides/metabolismo , Acetilação , Alanina/metabolismo , Proteínas de Arabidopsis/química , Clorofila/metabolismo , Proteínas de Ligação a DNA/química , Luz , Complexos de Proteínas Captadores de Luz/metabolismo , Modelos Biológicos , Fosforilação , Fosfotreonina/metabolismo , Complexo de Proteína do Fotossistema I/química , Complexo de Proteína do Fotossistema II/metabolismo , Ligação Proteica , Isoformas de Proteínas/metabolismo , Subunidades Proteicas/metabolismo
Plant Physiol ; 180(3): 1582-1597, 2019 07.
Artigo em Inglês | MEDLINE | ID: mdl-31061101


In all eukaryotes, protein phosphorylation is a key regulatory mechanism in several cellular processes, including the acclimation of photosynthesis to environmental cues. Despite being a well-conserved regulatory mechanism in the chloroplasts of land plants, distinct differences in thylakoid protein phosphorylation patterns have emerged from studies on species of different phylogenetic groups. Here, we analyzed thylakoid protein phosphorylation in the moss Physcomitrella patens, assessing the thylakoid phospho-protein profile and dynamics in response to changes in white light intensity. Compared with Arabidopsis (Arabidopsis thaliana), parallel characterization of wild-type P patens and the knockout mutant stn8 (depleted in SER/THR PROTEIN KINASE8 [STN8]) disclosed a moss-specific pattern of thylakoid protein phosphorylation, both with respect to specific targets and to their dynamic phosphorylation in response to environmental cues. Unlike vascular plants, (1) phosphorylation of the PSII protein D1 in P patens was negligible under all light conditions, (2) phosphorylation of the PSII core subunits CP43 and D2 showed only minor changes upon fluctuations in light intensity, and (3) absence of STN8 completely abolished all PSII core protein phosphorylation. Further, we detected light-induced phosphorylation in the minor light harvesting complex (LHC) antenna protein LHCB6, which was dependent on STN8 kinase activity, and found specific phosphorylations on LHCB3. Data presented here provide further insights into the appearance and physiological role of thylakoid protein phosphorylation during evolution of oxygenic photosynthetic organisms and their colonization of land.

Bryopsida/metabolismo , Cloroplastos/metabolismo , Proteínas de Plantas/metabolismo , Proteínas Serina-Treonina Quinases/metabolismo , Tilacoides/metabolismo , Arabidopsis/genética , Arabidopsis/metabolismo , Bryopsida/genética , Cloroplastos/genética , Cloroplastos/ultraestrutura , Cinética , Luz , Complexos de Proteínas Captadores de Luz/genética , Complexos de Proteínas Captadores de Luz/metabolismo , Microscopia Eletrônica de Transmissão , Mutação , Fosforilação , Fotossíntese/genética , Fotossíntese/efeitos da radiação , Complexo de Proteína do Fotossistema II/genética , Complexo de Proteína do Fotossistema II/metabolismo , Proteínas de Plantas/genética , Proteínas Quinases/genética , Proteínas Quinases/metabolismo , Proteínas Serina-Treonina Quinases/genética , Tilacoides/genética , Tilacoides/ultraestrutura