scholarly journals Zeaxanthin Binds to Light-Harvesting Complex Stress-Related Protein to Enhance Nonphotochemical Quenching in Physcomitrella patens

2013 ◽  
Vol 25 (9) ◽  
pp. 3519-3534 ◽  
Author(s):  
Alberta Pinnola ◽  
Luca Dall’Osto ◽  
Caterina Gerotto ◽  
Tomas Morosinotto ◽  
Roberto Bassi ◽  
...  
Keyword(s):  
Physcomitrella Patens ◽  
Light Harvesting ◽  
Complex Stress ◽  
Nonphotochemical Quenching ◽  
Related Protein ◽  
Light Harvesting Complex

scholarly journals Light-Harvesting Complex Stress-Related Proteins Catalyze Excess Energy Dissipation in Both Photosystems of Physcomitrella patens

2015 ◽  
Vol 27 (11) ◽  
pp. 3213-3227 ◽  
Author(s):  
Alberta Pinnola ◽  
Stefano Cazzaniga ◽  
Alessandro Alboresi ◽  
Reinat Nevo ◽  
Smadar Levin-Zaidman ◽  
...  
Keyword(s):  
Energy Dissipation ◽  
Physcomitrella Patens ◽  
Light Harvesting ◽  
Complex Stress ◽  
Excess Energy ◽  
Light Harvesting Complex ◽  
Related Proteins

scholarly journals An atypical member of the light-harvesting complex stress-related protein family modulates diatom responses to light

2010 ◽  
Vol 107 (42) ◽  
pp. 18214-18219 ◽  
Author(s):  
B. Bailleul ◽  
A. Rogato ◽  
A. de Martino ◽  
S. Coesel ◽  
P. Cardol ◽  
...  
Keyword(s):  
Light Harvesting ◽  
Complex Stress ◽  
Protein Family ◽  
Related Protein ◽  
Light Harvesting Complex ◽  
Atypical Member

scholarly journals pH dependence, kinetics and light-harvesting regulation of nonphotochemical quenching inChlamydomonas

2019 ◽  
Vol 116 (17) ◽  
pp. 8320-8325 ◽  
Author(s):  
Lijin Tian ◽  
Wojciech J. Nawrocki ◽  
Xin Liu ◽  
Iryna Polukhina ◽  
Ivo H. M. van Stokkum ◽  
...  
Keyword(s):  
Light Harvesting ◽  
Ph Dependence ◽  
Ph Sensor ◽  
Complex Stress ◽  
Nonphotochemical Quenching ◽  
Ps Ii ◽  
Light Harvesting Complex ◽  
Photosynthetic Organisms

Sunlight drives photosynthesis but can also cause photodamage. To protect themselves, photosynthetic organisms dissipate the excess absorbed energy as heat, in a process known as nonphotochemical quenching (NPQ). In green algae, diatoms, and mosses, NPQ depends on the light-harvesting complex stress-related (LHCSR) proteins. Here we investigated NPQ inChlamydomonas reinhardtiiusing an approach that maintains the cells in a stable quenched state. We show that in the presence of LHCSR3, all of the photosystem (PS) II complexes are quenched and the LHCs are the site of quenching, which occurs at a rate of ∼150 ps−1and is not induced by LHCII aggregation. The effective light-harvesting capacity of PSII decreases upon NPQ, and the NPQ rate is independent of the redox state of the reaction center. Finally, we could measure the pH dependence of NPQ, showing that the luminal pH is always above 5.5 in vivo and highlighting the role of LHCSR3 as an ultrasensitive pH sensor.

scholarly journals Identification of parallel pH- and zeaxanthin-dependent quenching of excess energy in LHCSR3 in Chlamydomonas reinhardtii

2020 ◽  
Author(s):  
Julianne M. Troiano ◽  
Federico Perozeni ◽  
Raymundo Moya ◽  
Luca Zuliani ◽  
Kwangryul Baek ◽  
...  
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Light Harvesting ◽  
Complex Stress ◽  
Excess Energy ◽  
Photochemical Quenching ◽  
Light Harvesting Complexes ◽  
Light Harvesting Complex ◽  
Non Photochemical Quenching

AbstractUnder high light conditions, oxygenic photosynthetic organisms avoid photodamage by thermally dissipating excess absorbed energy, which is called non-photochemical quenching (NPQ). In green algae, a chlorophyll and carotenoid-binding protein, light-harvesting complex stress-related (LHCSR3), detects excess energy via pH and serves as a quenching site. However, the mechanisms by which LHCSR3 functions have not been determined. Using a combined in vivo and in vitro approach, we identify two parallel yet distinct quenching processes, individually controlled by pH and carotenoid composition, and their likely molecular origin within LHCSR3 from Chlamydomonas reinhardtii. The pH-controlled quenching is removed within a mutant LHCSR3 that lacks the protonable residues responsible for sensing pH. Constitutive quenching in zeaxanthin-enriched systems demonstrates zeaxanthin-controlled quenching, which may be shared with other light-harvesting complexes. We show that both quenching processes prevent the formation of damaging reactive oxygen species, and thus provide distinct timescales and mechanisms of protection in a changing environment.

scholarly journals Structure of the stress-related LHCSR1 complex determined by an integrated computational strategy

2021 ◽  
Author(s):  
Ingrid Guarnetti Prandi ◽  
Vladislav Sláma ◽  
Cristina Pecorilla ◽  
Lorenzo Cupellini ◽  
Benedetta Mennucci
Keyword(s):  
Structural Model ◽  
Light Harvesting ◽  
Structural Information ◽  
Protein Complexes ◽  
Complex Stress ◽  
Main Function ◽  
Light Harvesting Complexes ◽  
Light Harvesting Complex ◽  
Pigment Protein Complexes ◽  
Computational Strategy

Light-harvesting complexes (LHCs) are pigment-protein complexes whose main function is to capture sunlight and transfer the energy to reaction centers of photosystems. In response to varying light conditions, LH complexes also play photoregulation and photoprotection roles. In algae and mosses, a sub-family of LHCs, Light-Harvesting complex stress related (LHCSR), is responsible for photoprotective quenching. Despite their functional and evolutionary importance, no direct structural information on LHCSRs is available that can explain their unique properties. In this work we propose a structural model of LHCSR1 from the moss P. Patens, obtained through an integrated computational strategy that combines homology modeling, molecular dynamics, and multiscale quantum chemical calculations. The model is validated by reproducing the spectral properties of LHCSR1. Our model reveals the structural specificity of LHCSR1, as compared with the CP29 LH complex, and poses the basis for understanding photoprotective quenching in mosses.

scholarly journals Microsecond and millisecond dynamics in the photosynthetic protein LHCSR1 observed by single-molecule correlation spectroscopy

2019 ◽  
Vol 116 (23) ◽  
pp. 11247-11252 ◽  
Author(s):  
Toru Kondo ◽  
Jesse B. Gordon ◽  
Alberta Pinnola ◽  
Luca Dall’Osto ◽  
Roberto Bassi ◽  
...  
Keyword(s):  
Correlation Function ◽  
Single Molecule ◽  
Conformational Changes ◽  
Protein Function ◽  
Light Harvesting ◽  
Building Blocks ◽  
Complex Stress ◽  
Correlation Spectroscopy ◽  
Light Harvesting Complex ◽  
Single Molecule Level

Biological systems are subjected to continuous environmental fluctuations, and therefore, flexibility in the structure and function of their protein building blocks is essential for survival. Protein dynamics are often local conformational changes, which allows multiple dynamical processes to occur simultaneously and rapidly in individual proteins. Experiments often average over these dynamics and their multiplicity, preventing identification of the molecular origin and impact on biological function. Green plants survive under high light by quenching excess energy, and Light-Harvesting Complex Stress Related 1 (LHCSR1) is the protein responsible for quenching in moss. Here, we expand an analysis of the correlation function of the fluorescence lifetime by improving the estimation of the lifetime states and by developing a multicomponent model correlation function, and we apply this analysis at the single-molecule level. Through these advances, we resolve previously hidden rapid dynamics, including multiple parallel processes. By applying this technique to LHCSR1, we identify and quantitate parallel dynamics on hundreds of microseconds and tens of milliseconds timescales, likely at two quenching sites within the protein. These sites are individually controlled in response to fluctuations in sunlight, which provides robust regulation of the light-harvesting machinery. Considering our results in combination with previous structural, spectroscopic, and computational data, we propose specific pigments that serve as the quenching sites. These findings, therefore, provide a mechanistic basis for quenching, illustrating the ability of this method to uncover protein function.

scholarly journals UV-B photoreceptor-mediated protection of the photosynthetic machinery inChlamydomonas reinhardtii

2016 ◽  
Vol 113 (51) ◽  
pp. 14864-14869 ◽  
Author(s):  
Guillaume Allorent ◽  
Linnka Lefebvre-Legendre ◽  
Richard Chappuis ◽  
Marcel Kuntz ◽  
Thuy B. Truong ◽  
...  
Keyword(s):  
Photosynthetic Activity ◽  
Light Harvesting ◽  
Nonphotochemical Quenching ◽  
High Light ◽  
Light Energy ◽  
Light Harvesting Complex ◽  
Subsequent Exposure ◽  
Photosynthetic Machinery ◽  
Life On Earth ◽  
Energy Dependent

Life on earth is dependent on the photosynthetic conversion of light energy into chemical energy. However, absorption of excess sunlight can damage the photosynthetic machinery and limit photosynthetic activity, thereby affecting growth and productivity. Photosynthetic light harvesting can be down-regulated by nonphotochemical quenching (NPQ). A major component of NPQ is qE (energy-dependent nonphotochemical quenching), which allows dissipation of light energy as heat. Photodamage peaks in the UV-B part of the spectrum, but whether and how UV-B induces qE are unknown. Plants are responsive to UV-B via the UVR8 photoreceptor. Here, we report in the green algaChlamydomonas reinhardtiithat UVR8 induces accumulation of specific members of the light-harvesting complex (LHC) superfamily that contribute to qE, in particular LHC Stress-Related 1 (LHCSR1) and Photosystem II Subunit S (PSBS). The capacity for qE is strongly induced by UV-B, although the patterns of qE-related proteins accumulating in response to UV-B or to high light are clearly different. The competence for qE induced by acclimation to UV-B markedly contributes to photoprotection upon subsequent exposure to high light. Our study reveals an anterograde link between photoreceptor-mediated signaling in the nucleocytosolic compartment and the photoprotective regulation of photosynthetic activity in the chloroplast.

scholarly journals LHCSR3 is a nonphotochemical quencher of both photosystems inChlamydomonas reinhardtii

2019 ◽  
Vol 116 (10) ◽  
pp. 4212-4217 ◽  
Author(s):  
Laura Girolomoni ◽  
Stefano Cazzaniga ◽  
Alberta Pinnola ◽  
Federico Perozeni ◽  
Matteo Ballottari ◽  
...  
Keyword(s):  
Light Harvesting ◽  
Internal Standard ◽  
Green Fluorescence Protein ◽  
Complex Stress ◽  
Antenna System ◽  
Thermal Dissipation ◽  
Light Harvesting Complexes ◽  
Light Harvesting Complex ◽  
Whole Cells ◽  
Photosynthetic Organisms

Photosynthetic organisms prevent oxidative stress from light energy absorbed in excess through several photoprotective mechanisms. A major component is thermal dissipation of chlorophyll singlet excited states and is called nonphotochemical quenching (NPQ). NPQ is catalyzed in green algae by protein subunits called LHCSRs (Light Harvesting Complex Stress Related), homologous to the Light Harvesting Complexes (LHC), constituting the antenna system of both photosystem I (PSI) and PSII. We investigated the role of LHCSR1 and LHCSR3 in NPQ activation to verify whether these proteins are involved in thermal dissipation of PSI excitation energy, in addition to their well-known effect on PSII. To this aim, we measured the fluorescence emitted at 77 K by whole cells in a quenched or unquenched state, using green fluorescence protein as the internal standard. We show that NPQ activation by high light treatment inChlamydomonas reinhardtiileads to energy quenching in both PSI and PSII antenna systems. By analyzing quenching properties of mutants affected on the expression of LHCSR1 or LHCSR3 gene products and/or state 1–state 2 transitions or zeaxanthin accumulation, namely,npq4,stt7,stt7 npq4,npq4 lhcsr1,lhcsr3-complementednpq4 lhcsr1andnpq1, we showed that PSI undergoes NPQ through quenching of the associated LHCII antenna. This quenching event is fast-reversible on switching the light off, is mainly related to LHCSR3 activity, and is dependent on thylakoid luminal pH. Moreover, PSI quenching could also be observed in the absence of zeaxanthin or STT7 kinase activity.

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