Role of Calcium Ions in Motility and Phototaxis of Chlamydomonas reinhardtii

1987 ◽  
Vol 126 (4-5) ◽  
pp. 467-473 ◽  
Author(s):  
Reiner Dolle ◽  
Jürgen Pfau ◽  
Wilhelm Nultsch
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Calcium Ions

Mitochondrial matrix calcium ions regulate energy production in myocardium: A cytochemical study

1990 ◽  
Vol 48 (2) ◽  
pp. 166-167
Author(s):  
W.A. Jacob ◽  
R. Hertsens ◽  
A. Van Bogaert ◽  
M. De Smet
Keyword(s):  
Energy Metabolism ◽  
Calcium Ions ◽  
Energy Production ◽  
Regulation Of Respiration ◽  
Free Calcium ◽  
Mitochondrial Matrix ◽  
Cytochemical Study ◽  
Nmr Techniques

In the past most studies of the control of energy metabolism focus on the role of the phosphorylation potential ATP/ADP.Pi on the regulation of respiration. Studies using NMR techniques have demonstrated that the concentrations of these compounds for oxidation phosphorylation do not change appreciably throughout the cardiac cycle and during increases in cardiac work. Hence regulation of energy production by calcium ions, present in the mitochondrial matrix, has been the object of a number of recent studies.Three exclusively intramitochondnal dehydrogenases are key enzymes for the regulation of oxidative metabolism. They are activated by calcium ions in the low micromolar range. Since, however, earlier estimates of the intramitochondnal calcium, based on equilibrium thermodynamic considerations, were in the millimolar range, a physiological correlation was not evident. The introduction of calcium-sensitive probes fura-2 and indo-1 made monitoring of free calcium during changing energy metabolism possible. These studies were performed on isolated mitochondria and extrapolation to the in vivo situation is more or less speculative.

scholarly journals The Role of Acidic Residues in the C Terminal Tail of the LHCSR3 Protein of Chlamydomonas reinhardtii in Non-Photochemical Quenching

2021 ◽  
pp. 6895-6900
Author(s):  
Franco V. A. Camargo ◽  
Federico Perozeni ◽  
Gabriel de la Cruz Valbuena ◽  
Luca Zuliani ◽  
Samim Sardar ◽  
...  
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Photochemical Quenching ◽  
Acidic Residues ◽  
Non Photochemical Quenching

Non-photochemical quenching of chlorophyll a fluorescence: early history and characterization of two xanthophyll-cycle mutants of Chlamydomonas reinhardtii

2002 ◽  
Vol 29 (10) ◽  
pp. 1141 ◽  
Author(s):  
Govindjee ◽  
Manfredo J. Seufferheld
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Oxygen Evolution ◽  
Xanthophyll Cycle ◽  
Photochemical Quenching ◽  
Chl A ◽  
Fluorescence Transient ◽  
Chl A Fluorescence ◽  
Non Photochemical Quenching

This paper deals first with the early, although incomplete, history of photoinhibition, of 'non-QA-related chlorophyll (Chl) a fluorescence changes', and the xanthophyll cycle that preceded the discovery of the correlation between non-photochemical quenching of Chl a fluorescence (NPQ) and conversion of violaxanthin to zeaxanthin. It includes the crucial observation that the fluorescence intensity quenching, when plants are exposed to excess light, is indeed due to a change in the quantum yield of fluorescence. The history ends with a novel turn in the direction of research — isolation and characterization of NPQ xanthophyll-cycle mutants of Chlamydomonas reinhardtii Dangeard and Arabidopsis thaliana (L.) Heynh., blocked in conversion of violaxanthin to zeaxanthin, and zeaxanthin to violaxanthin, respectively. In the second part of the paper, we extend the characterization of two of these mutants (npq1, which accumulates violaxanthin, and npq2, which accumulates zeaxanthin) through parallel measurements on growth, and several assays of PSII function: oxygen evolution, Chl a fluorescence transient (the Kautsky effect), the two-electron gate function of PSII, the back reactions around PSII, and measurements of NPQ by pulse-amplitude modulation (PAM 2000) fluorimeter. We show that, in the npq2 mutant, Chl a fluorescence is quenched both in the absence and presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU). However, no differences are observed in functioning of the electron-acceptor side of PSII — both the two-electron gate and the back reactions are unchanged. In addition, the role of protons in fluorescence quenching during the 'P-to-S' fluorescence transient was confirmed by the effect of nigericin in decreasing this quenching effect. Also, the absence of zeaxanthin in the npq1 mutant leads to reduced oxygen evolution at high light intensity, suggesting another protective role of this carotenoid. The available data not only support the current model of NPQ that includes roles for both pH and the xanthophylls, but also are consistent with additional protective roles of zeaxanthin. However, this paper emphasizes that we still lack sufficient understanding of the different parts of NPQ, and that the precise mechanisms of photoprotection in the alga Chlamydomonas may not be the same as those in higher plants.

Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism

2001 ◽  
Vol 359 (1) ◽  
pp. 65-75 ◽  
Author(s):  
Valeria MENCHISE ◽  
Catherine CORBIER ◽  
Claude DIDIERJEAN ◽  
Michele SAVIANO ◽  
Ettore BENEDETTI ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Proton Transfer ◽  
Chlamydomonas Reinhardtii ◽  
Catalytic Mechanism ◽  
Structural Data ◽  
Careful Analysis ◽  
Wild Type ◽  
Thioredoxin H ◽  
Dynamics Simulations

Thioredoxins are ubiquitous proteins which catalyse the reduction of disulphide bridges on target proteins. The catalytic mechanism proceeds via a mixed disulphide intermediate whose breakdown should be enhanced by the involvement of a conserved buried residue, Asp-30, as a base catalyst towards residue Cys-39. We report here the crystal structure of wild-type and D30A mutant thioredoxin h from Chlamydomonas reinhardtii, which constitutes the first crystal structure of a cytosolic thioredoxin isolated from a eukaryotic plant organism. The role of residue Asp-30 in catalysis has been revisited since the distance between the carboxylate OD1 of Asp-30 and the sulphur SG of Cys-39 is too great to support the hypothesis of direct proton transfer. A careful analysis of all available crystal structures reveals that the relative positioning of residues Asp-30 and Cys-39 as well as hydrophobic contacts in the vicinity of residue Asp-30 do not allow a conformational change sufficient to bring the two residues close enough for a direct proton transfer. This suggests that protonation/deprotonation of Cys-39 should be mediated by a water molecule. Molecular-dynamics simulations, carried out either in vacuo or in water, as well as proton-inventory experiments, support this hypothesis. The results are discussed with respect to biochemical and structural data.

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.

Sign in / Sign up

Export Citation Format

Share Document