Synthesis of an Atrazine-Binding Protein of the PSII Reaction Center in Isolated Wheat Etiochloroplasts

1987 ◽  
Keyword(s):  
Reaction Center ◽  
Binding Protein ◽  
Psii Reaction Center

Role of an Extrinsic 33 Kilodalton Protein of Photosystem II in the Turnover of the Reaction Center-Binding Protein D1 during Photoinhibition†

Biochemistry ◽  
1998 ◽  
Vol 37 (6) ◽  
pp. 1565-1574 ◽  
Author(s):  
Yasusi Yamamoto ◽  
Yasuo Ishikawa ◽  
Etsuko Nakatani ◽  
Mina Yamada ◽  
Haoming Zhang ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Binding Protein

scholarly journals Exploring the Link between Photosystem II Assembly and Translation of the Chloroplast psbA mRNA

Plants ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 152 ◽  
Author(s):  
Prakitchai Chotewutmontri ◽  
Rosalind Williams-Carrier ◽  
Alice Barkan
Keyword(s):  
Photosystem Ii ◽  
Water Splitting ◽  
Reaction Center ◽  
Ribosome Profiling ◽  
Oxygenic Photosynthesis ◽  
Dual Roles ◽  
Psii Reaction Center ◽  
Core Proteins ◽  
Prosthetic Groups ◽  
Autoregulatory Mechanism

Photosystem II (PSII) in chloroplasts and cyanobacteria contains approximately fifteen core proteins, which organize numerous pigments and prosthetic groups that mediate the light-driven water-splitting activity that drives oxygenic photosynthesis. The PSII reaction center protein D1 is subject to photodamage, whose repair requires degradation of damaged D1 and its replacement with nascent D1. Mechanisms that couple D1 synthesis with PSII assembly and repair are poorly understood. We address this question by using ribosome profiling to analyze the translation of chloroplast mRNAs in maize and Arabidopsis mutants with defects in PSII assembly. We found that OHP1, OHP2, and HCF244, which comprise a recently elucidated complex involved in PSII assembly and repair, are each required for the recruitment of ribosomes to psbA mRNA, which encodes D1. By contrast, HCF136, which acts upstream of the OHP1/OHP2/HCF244 complex during PSII assembly, does not have this effect. The fact that the OHP1/OHP2/HCF244 complex brings D1 into proximity with three proteins with dual roles in PSII assembly and psbA ribosome recruitment suggests that this complex is the hub of a translational autoregulatory mechanism that coordinates D1 synthesis with need for nascent D1 during PSII biogenesis and repair.

scholarly journals Involvement of Carboxyl Groups of the PSII Reaction Center Proteins in Photoactivation of the Apo-Water-Oxidizing Complex

1997 ◽  
Vol 38 (5) ◽  
pp. 578-585 ◽  
Author(s):  
N. Tamura ◽  
K. Noda ◽  
K. Wakamatsu ◽  
H. Kamachi ◽  
H. Inoue ◽  
...  
Keyword(s):  
Reaction Center ◽  
Carboxyl Groups ◽  
Psii Reaction Center ◽  
Water Oxidizing Complex

Effects of water stress and rewatering on turnover and gene expression of photosystem II reaction center polypeptide D1 in Zea mays

1999 ◽  
Vol 26 (4) ◽  
pp. 375 ◽  
Author(s):  
Limin Hao ◽  
Houguo Liang ◽  
Zongling Wang ◽  
Xinmin Liu
Keyword(s):  
Water Stress ◽  
Electron Transport ◽  
Photosystem Ii ◽  
Reaction Center ◽  
Control Level ◽  
State Level ◽  
Transcript Level ◽  
Dot Blot ◽  
Psii Reaction Center ◽  
Severe Water Stress

Photosystem II oxygen evolution capacity, the steady-state level of photosystem II (PSII) reaction center polypeptide D1 and its transcript and template levels inZea mays L. (Xinyu No. 4) under water stress and rewatering were studied. The results indicated that PSII and whole-chain electron transport capacities decreased slightly under moderate water stress and appreciably under severe water stress, and could not recover to control level upon rewatering. The results of western and northern blots showed that the content of PSII reaction center polypeptide D1 changed as a similar pattern to PSII and whole-chain electron transport capacities. Dot blot analysis for DNA showed that there was no obvious response of the template level of D1 to water stress or rewatering. From the results, it was concluded that PSII was the major site affected by water stress, where the functional loss of PSII could be attributed to the reduction of PSII reaction center polypeptide D1, which may be caused by the decrease in its transcript level. Rewatering could only ameliorate slightly under moderate water stress but could not recover to control level under severe water stress.

scholarly journals Translation of the Chloroplast psbA mRNA Requires the Nuclear-encoded Poly(A)-binding Protein, RB47

1998 ◽  
Vol 142 (2) ◽  
pp. 435-442 ◽  
Author(s):  
Christopher B. Yohn ◽  
Amybeth Cohen ◽  
Cristen Rosch ◽  
Michael R. Kuchka ◽  
Stephen P. Mayfield
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Untranslated Region ◽  
Translational Regulation ◽  
Rna Binding ◽  
Binding Protein ◽  
Biochemical Data ◽  
Cohesive Model ◽  
High Affinity ◽  
Translational Activator

A set of nuclear mutants of C. reinhardtii were identified that specifically lack translation of the chloroplast-encoded psbA mRNA, which encodes the photosystem II reaction center polypeptide D1. Two of these mutants are deficient in the 47-kD member (RB47) of the psbA RNA-binding complex, which has previously been identified both genetically and biochemically as a putative translational activator of the chloroplast psbA mRNA. RB47 is a member of the poly(A)-binding protein family, and binds with high affinity and specificity to the 5′ untranslated region of the psbA mRNA. The results presented here confirm RB47's role as a message-specific translational activator in the chloroplast, and bring together genetic and biochemical data to form a cohesive model for light- activated translational regulation in the chloroplast.

Inhibition of Photosystem II by UV-B-Radiation

1985 ◽  
Vol 40 (1-2) ◽  
pp. 129-133 ◽  
Author(s):  
M. Tevini ◽  
K. Pfister
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Mathematical Analysis ◽  
Binding Protein ◽  
Donor Site ◽  
Fluorescence Induction ◽  
Spinach Chloroplasts ◽  
Psii Activity ◽  
Herbicide Binding

Abstract The effect of UV-B-radiation on PSII activity of spinach chloroplasts was analyzed by measuring the integrity of the herbicide-binding protein (HBP 32), by measurement of fluorescence induction in the presence of Diuron (DCMU), and by mathematical analysis of the fluorescence induction curves. It was shown that UV-B inactivates the PSII α-centers but not PSII β-centers. However, the possibility cannot be excluded that in addition the donor site of PSII near the reaction center is attacked by UV-B-radiation.

scholarly journals Chlorophyll Composition, Chlorophyll Fluorescence, and Grain Yield Change in esl Mutant Rice

2018 ◽  
Vol 19 (10) ◽  
pp. 2945 ◽  
Author(s):  
Weiwei Lin ◽  
Xiaodong Guo ◽  
Xinfeng Pan ◽  
Zhaowei Li
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Binding Protein ◽  
Grain Filling ◽  
Fluorescence Yield ◽  
Light Energy ◽  
Grain Weight ◽  
Filling Stage ◽  
Grain Filling Stage ◽  
1000 Grain Weight

To evaluate the effect of changes in chlorophyll (Chl) composition and fluorescence on final yield formation, early senescence leaf (esl) mutant rice and its wild-type cultivar were employed to investigate the genotype-dependent differences in Chl composition, Chl fluorescence, and yield characteristics during the grain-filling stage. However, the temporal expression patterns of key genes involved in the photosystem II (PSII) reaction center in the leaves of two rice genotypes were analyzed by quantitative real-time polymerase chain reaction (qRT-PCR). Results showed that the seed-setting rate, 1000-grain weight, and yield per plant remarkably decreased, and the increase in the 1000-grain weight during the grain-filling stage was retarded in esl mutant rice. Chl composition, maximal fluorescence yield (Fm), variable fluorescence (Fv), a maximal quantum yield of PSII photochemistry (Fv/Fm), and net photosynthetic rate (Pn) in esl mutant rice considerably decreased, thereby indicating the weakened abilities of light energy harvesting and transferring in senescent leaves. The esl mutant rice showed an increase in the minimal fluorescence yield (F0) and 1 − Fv/Fm and decreases in the expression levels of light-harvesting Chl a/b binding protein (Cab) and photosystem II binding protein A (PsbA), PsbB, PsbC, and PsbD encoding for the reaction center of the PSII complex during the grain-filling stage. These results indicated the PSII reaction centers were severely damaged in the mesophyll cells of senescent leaves, which resulted in the weakened harvesting quantum photon and transferring light energy to PSI and PSII for carbon dioxide assimilation, leading to enhanced heat dissipation of light energy and a decrease in Pn.

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