Pigment protein complexes and functional properties of tetratype resulting from crosses between CP1 and CP2 less Chlamydomonas mutants

1986 ◽  
Vol 7 (3) ◽  
pp. 221-236 ◽  
Author(s):  
A. Picaud ◽  
G. Dubertret
Keyword(s):  
Functional Properties ◽  
Protein Complexes ◽  
Pigment Protein Complexes ◽  
Chlamydomonas Mutants

Carotenoidless pigment-protein complexes of the sulfur photosynthetic bacterium Ectothiorhodospira haloalkaliphila

2013 ◽  
Vol 453 (1) ◽  
pp. 304-307 ◽  
Author(s):  
A. A. Ashikhmin ◽  
Yu. E. Erokhin ◽  
Z. K. Makhneva ◽  
A. A. Moskalenko
Keyword(s):  
Protein Complexes ◽  
Photosynthetic Bacterium ◽  
Pigment Protein Complexes

Biogenesis of Chloroplasts and Pigment-Protein Complexes in Barley Seedlings with Blocked Biosynthesis of Carotenoids

1992 ◽  
pp. 349-354
Author(s):  
Navassard V. Karapetyan ◽  
Marina G. Rakhimberdieva ◽  
Yulia V. Bolychevtseva ◽  
Andrei A. Moskalenko ◽  
Nina Yu. Kuznetsova ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Pigment Protein Complexes

scholarly journals The role of LHCBM1 in non-photochemical quenching in Chlamydomonas reinhardtii

2022 ◽  
Author(s):  
Xin Liu ◽  
Wojciech J Nawrocki ◽  
Roberta Croce
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Protein Complexes ◽  
Ph Sensor ◽  
High Light ◽  
Photochemical Quenching ◽  
Knock Out ◽  
Photosynthetic Organisms ◽  
Pigment Protein Complexes ◽  
Non Photochemical Quenching

Non-photochemical quenching (NPQ) is the process that protects photosynthetic organisms from photodamage by dissipating the energy absorbed in excess as heat. In the model green alga Chlamydomonas reinhardtii, NPQ was abolished in the knock-out mutants of the pigment-protein complexes LHCSR3 and LHCBM1. However, while LHCSR3 was shown to be a pH sensor and switching to a quenched conformation at low pH, the role of LHCBM1 in NPQ has not been elucidated yet. In this work, we combine biochemical and physiological measurements to study short-term high light acclimation of npq5, the mutant lacking LHCBM1. We show that while in low light in the absence of this complex, the antenna size of PSII is smaller than in its presence, this effect is marginal in high light, implying that a reduction of the antenna is not responsible for the low NPQ. We also show that the mutant expresses LHCSR3 at the WT level in high light, indicating that the absence of this complex is also not the reason. Finally, NPQ remains low in the mutant even when the pH is artificially lowered to values that can switch LHCSR3 to the quenched conformation. It is concluded that both LHCSR3 and LHCBM1 need to be present for the induction of NPQ and that LHCBM1 is the interacting partner of LHCSR3. This interaction can either enhance the quenching capacity of LHCSR3 or connect this complex with the PSII supercomplex.

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.

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