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

The rise and fall of Light-Harvesting Complex Stress-Related proteins as photoprotection agents during evolution

2019 ◽  
Vol 70 (20) ◽  
pp. 5527-5535 ◽  
Author(s):  
Alberta Pinnola
Keyword(s):  
Vascular Plants ◽  
Light Harvesting ◽  
Complex Stress ◽  
Excess Energy ◽  
Light Harvesting Complex ◽  
Quenching Mechanisms ◽  
Related Proteins ◽  
Role Of Light ◽  
Psbs Protein

This review on the evolution of quenching mechanisms for excess energy dissipation focuses on the role of Light-Harvesting Complex Stress-Related (LHCSR) proteins versus Photosystem II Subunit S (PSBS) protein, and the reasons for the redundancy of LHCSR in vascular plants as PSBS became established.

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 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 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 Energy dissipation mechanisms in the FCPb light-harvesting complex of the diatom Cyclotella meneghiniana

2018 ◽  
Vol 1859 (10) ◽  
pp. 1151-1160 ◽  
Author(s):  
Huzifa M.A.M. Elnour ◽  
Lars Dietzel ◽  
Charusheela Ramanan ◽  
Claudia Büchel ◽  
Rienk van Grondelle ◽  
...  
Keyword(s):  
Energy Dissipation ◽  
Light Harvesting ◽  
Light Harvesting Complex ◽  
Cyclotella Meneghiniana

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 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
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