Simultaneous regulation of antenna size and photosystem I/II stoichiometry in Arabidopsis thaliana

Jia, Ting; Itô, Hisashi; Tanaka, Ayumi

doi:10.1007/s00425-016-2568-5

Cited by 27 publications

(21 citation statements)

References 68 publications

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“…A near equimolar stoichiometry was also found within the photosystem I core between P700 chlorophyll apoprotein A1 and A2 (PsaA and PsaB) (Figure 2c,d ). Noticeably, PSII reaction centres were 3–4 times more abundant than PSI reaction centres, as reported earlier to be the case for higher plant chloroplasts (Jia, Ito, & Tanaka, 2016 ; Koskela et al, 2020 ). This highlights the potential for this data to be used as a basis for further functional exploration of complex enzymatic processes that require knowledge of enzyme abundances and stoichiometries, possibly at the systems biology scale.…”

Section: Resultssupporting

confidence: 77%

Quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance

Guihur

Fauvet

Finka

et al. 2020

Plant Cell & Environment

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At dawn of a scorching summer day, land plants must anticipate upcoming extreme midday temperatures by timely establishing molecular defences that can keep heat‐labile membranes and proteins functional. A gradual morning pre‐exposure to increasing sub‐damaging temperatures induces heat‐shock proteins (HSPs) that are central to the onset of plant acquired thermotolerance (AT). To gain knowledge on the mechanisms of AT in the model land plant Physcomitrium patens, we used label‐free LC–MS/MS proteomics to quantify the accumulated and depleted proteins before and following a mild heat‐priming treatment. High protein crowding is thought to promote protein aggregation, whereas molecular chaperones prevent and actively revert aggregation. Yet, we found that heat priming (HP) did not accumulate HSP chaperones in chloroplasts, although protein crowding was six times higher than in the cytosol. In contrast, several HSP20s strongly accumulated in the cytosol, yet contributing merely 4% of the net mass increase of heat‐accumulated proteins. This is in poor concordance with their presumed role at preventing the aggregation of heat‐labile proteins. The data suggests that under mild HP unlikely to affect protein stability. Accumulating HSP20s leading to AT, regulate the activity of rare and specific signalling proteins, thereby preventing cell death under noxious heat stress.

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Section: Resultssupporting

confidence: 77%

Quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance

Guihur

Fauvet

Finka

et al. 2020

Plant Cell & Environment

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“…Chl b occurs exclusively in LHCs, which function as peripheral antennae (Kunugi et al 2016 ). In green plants, the antenna size of PSII is determined by the amount of LHCII (Jansson 1994 ; Tanaka and Tanaka 2011 ) and levels of LHCII are highly correlated with the accumulation of Chl b (Bailey et al 2001 ; Jia et al 2016 ), which is synthesized from Chl a by chlorophyllide a oxygenase (Tanaka and Tanaka 2011 ; Yamasato et al 2005 ). When plants grow under low light intensities, Chl b synthesis is enhanced and the antenna size increases (Bailey et al 2001 ).…”

Section: Discussionmentioning

confidence: 99%

Why is chlorophyll b only used in light-harvesting systems?

2018

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Chlorophylls (Chl) are important pigments in plants that are used to absorb photons and release electrons. There are several types of Chls but terrestrial plants only possess two of these: Chls a and b. The two pigments form light-harvesting Chl a/b-binding protein complexes (LHC), which absorb most of the light. The peak wavelengths of the absorption spectra of Chls a and b differ by c. 20 nm, and the ratio between them (the a/b ratio) is an important determinant of the light absorption efficiency of photosynthesis (i.e., the antenna size). Here, we investigated why Chl b is used in LHCs rather than other light-absorbing pigments that can be used for photosynthesis by considering the solar radiation spectrum under field conditions. We found that direct and diffuse solar radiation (PAR and PAR, respectively) have different spectral distributions, showing maximum spectral photon flux densities (SPFD) at c. 680 and 460 nm, respectively, during the daytime. The spectral absorbance spectra of Chls a and b functioned complementary to each other, and the absorbance peaks of Chl b were nested within those of Chl a. The absorption peak in the short wavelength region of Chl b in the proteinaceous environment occurred at c. 460 nm, making it suitable for absorbing the PAR, but not suitable for avoiding the high spectral irradiance (SIR) waveband of PAR. In contrast, Chl a effectively avoided the high SPFD and/or high SIR waveband. The absorption spectra of photosynthetic complexes were negatively correlated with SPFD spectra, but LHCs with low a/b ratios were more positively correlated with SIR spectra. These findings indicate that the spectra of the photosynthetic pigments and constructed photosystems and antenna proteins significantly align with the terrestrial solar spectra to allow the safe and efficient use of solar radiation.

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“…Although a detailed structural and mechanistic model is still lacking for CAO, the gene sequence encodes putative binding domains for a Rieske-type [2Fe-2S] center and for a mononuclear non-heme iron. The true substrate could be Chl a, rather than Chlide a (249), which raises the intriguing possibility that CAO could use both free and protein-bound Chl a as substrates.…”

Section: The Biosynthesis Of Chls B D and Fmentioning

confidence: 99%

Biosynthesis of the modified tetrapyrroles—the pigments of life

Bryant

Hunter

Warren

2020

Journal of Biological Chemistry

198

164

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Modified tetrapyrroles are large macrocyclic compounds, consisting of diverse conjugation and metal chelation systems and imparting an array of colors to the biological structures that contain them. Tetrapyrroles represent some of the most complex small molecules synthesized by cells and are involved in many essential processes that are fundamental to life on Earth, including photosynthesis, respiration, and catalysis. These molecules are all derived from a common template through a series of enzyme-mediated transformations that alter the oxidation state of the macrocycle and also modify its size, its side-chain composition, and the nature of the centrally chelated metal ion. The different modified tetrapyrroles include chlorophylls, hemes, siroheme, corrins (including vitamin B12), coenzyme F430, heme d1, and bilins. After nearly a century of study, almost all of the more than 90 different enzymes that synthesize this family of compounds are now known, and expression of reconstructed operons in heterologous hosts has confirmed that most pathways are complete. Aside from the highly diverse nature of the chemical reactions catalyzed, an interesting aspect of comparative biochemistry is to see how different enzymes and even entire pathways have evolved to perform alternative chemical reactions to produce the same end products in the presence and absence of oxygen. Although there is still much to learn, our current understanding of tetrapyrrole biogenesis represents a remarkable biochemical milestone that is summarized in this review.

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Simultaneous regulation of antenna size and photosystem I/II stoichiometry in Arabidopsis thaliana

Cited by 27 publications

References 68 publications

Quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance

Quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance

Why is chlorophyll b only used in light-harvesting systems?

Biosynthesis of the modified tetrapyrroles—the pigments of life

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