Composition, phosphorylation and dynamic organization of photosynthetic protein complexes in plant thylakoid membrane

Rantala, Marjaana; Rantala, Sanna; Aro, Eva‐Mari

doi:10.1039/d0pp00025f

Cited by 63 publications

(43 citation statements)

References 145 publications

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“…The factors involved in changes in the thylakoid architecture are not fully known. Recent studies have illuminated three groups of proteins that may control the thylakoid architecture: thylakoid-localized ion transporter/channels (Finazzi et al, 2015), phosphatases and kinases (STN7 and STN8 kinases) (Fristedt & Vener, 2011;Fristedt et al, 2009;Wunder et al, 2013), or structural proteins like CURT1 localized in the grana margins (Armbruster et al, 2013;Puthiyaveetil et al, 2014) or RIQ (Yokoyama et al, 2016) that control thylakoid ultrastructure (see also Rantala et al (2020)). The lumenal width could increase by osmotic water influx due to light-driven acidification of the lumen, which may cause proton motive force-driven influx of ions.…”

Section: Discussionmentioning

confidence: 99%

Measuring the dynamic response of the thylakoid architecture in plant leaves by electron microscopy

Mukhopadhyay

Svoboda

et al. 2020

Plant Direct

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The performance of the photosynthesis machinery in plants, including light harvesting, electron transport, and protein repair, is controlled by structural changes in the thylakoid membrane system inside the chloroplasts. In particular, the structure of the stacked grana area of thylakoid membranes is highly dynamic, changing in response to different environmental cues such as light intensity. For example, the aqueous thylakoid lumen enclosed by thylakoid membranes in grana has been documented to swell in the presence of light. However, light‐induced alteration of the stromal gap in the stacked grana (partition gap) and of the unstacked stroma lamellae has not been well characterized. Light‐induced changes in the entire thylakoid membrane system, including the lumen in both stacked and unstacked domains as well as the partition gap, are presented here, and the functional implications are discussed. This structural analysis was made possible by development of a robust semi‐automated image analysis method combined with optimized plant tissue fixation techniques for transmission electron microscopy generating quantitative structural results for the analysis of thylakoid ultrastructure. Significance Statement A methodical pipeline ranging from optimized leaf tissue preparation for electron microscopy to quantitative image analysis was established. This methodical development was employed to study details of light‐induced changes in the plant thylakoid ultrastructure. It was found that the lumen of the entire thylakoid system (stacked and unstacked domains) undergoes light‐induced swelling, whereas adjacent membranes on the stroma side in stacked grana thylakoid approach each other.

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Section: Discussionmentioning

confidence: 99%

Measuring the dynamic response of the thylakoid architecture in plant leaves by electron microscopy

Mukhopadhyay

Svoboda

et al. 2020

Plant Direct

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“…LHCII is a family of pigment protein complexes (i.e., Lhcb) with similar structure and evolutionary relationship, which are formed by proteins encoded by nuclear genes and pigments [ 28 ]. LHCII accounts for nearly 50% of the pigments in photosynthetic membrane and about 1/3 of the proteins [ 29 ]. At present, it is generally believed that LHCII contains six proteins, among which Lhcb1, Lhcb2 and Lhcb3 are the main light harvesting complexes, mostly in the form of trimers, while Lhab4, Lhcb5 and Lhcb6 are the secondary light harvesting complexes as monomers [ 30 ].…”

Section: Introductionmentioning

confidence: 99%

PSII Activity Was Inhibited at Flowering Stage with Developing Black Bracts of Oat

Liu

Zhang

Sun

et al. 2021

IJMS

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The color of bracts generally turns yellow or black from green during cereal grain development. However, the impact of these phenotypic changes on photosynthetic physiology during black bract formation remains unclear. Two oat cultivars (Avena sativa L.), ‘Triple Crown’ and ‘Qinghai 444’, with yellow and black bracts, respectively, were found to both have green bracts at the heading stage, but started to turn black at the flowering stage and become blackened at the milk stage for ‘Qinghai 444’. Their photosynthetic characteristics were analyzed and compared, and the key genes, proteins and regulatory pathways affecting photosynthetic physiology were determined in ‘Triple Crown’ and ‘Qinghai 444’ bracts. The results show that the actual PSII photochemical efficiency and PSII electron transfer rate of ‘Qinghai 444’ bracts had no significant changes at the heading and milk stages but decreased significantly (p < 0.05) at the flowering stage compared with ‘Triple Crown’. The chlorophyll content decreased, the LHCII involved in the assembly of supercomplexes in the thylakoid membrane was inhibited, and the expression of Lhcb1 and Lhcb5 was downregulated at the flowering stage. During this critical stage, the expression of Bh4 and C4H was upregulated, and the biosynthetic pathway of p-coumaric acid using tyrosine and phenylalanine as precursors was also enhanced. Moreover, the key upregulated genes (CHS, CHI and F3H) of anthocyanin biosynthesis might complement the impaired PSII activity until recovered at the milk stage. These findings provide a new insight into how photosynthesis alters during the process of oat bract color transition to black.

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“…Moreover, the protein density in the thylakoid membrane can be as large as 70% (Haferkamp et al ., 2010), meaning that each complex is surrounded by other complexes with which it might or might not functionally interact. Some of these interactions are controlled via phosphorylation, which is induced by different environmental factors (Goldschmidt‐Clermont & Bassi, 2015; Rantala et al ., 2020). This makes the ‘photosystems’ dynamic entities which can change their composition and organization depending on the conditions.…”

Section: Introductionmentioning

confidence: 99%

Beyond ‘seeing is believing’: the antenna size of the photosystems in vivo

Croce

2020

New Phytologist

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Photosystems I and II are the central components of the solar energy conversion machinery in oxygenic photosynthesis. They are large functional units embedded in the photosynthetic membranes, where they harvest light and use its energy to drive electrons from water to NADPH. Their composition and organization change in response to different environmental conditions, making these complexes dynamic units. Some of the interactions between subunits survive purification, resulting in the well-defined structures that were recently resolved by cryo-electron microscopy. Other interactions instead are weak, preventing the possibility of isolating and thus studying these complexes in vitro. This review focuses on these supercomplexes of vascular plants, which at the moment cannot be 'seen' but that represent functional units in vivo. Dedication: This review is dedicated to the memory of Prof. Jan Anderson, a pioneer in this field, a great scientist, a great woman, an example for me.

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Composition, phosphorylation and dynamic organization of photosynthetic protein complexes in plant thylakoid membrane

Abstract: Here we present an overview of the composition and organization of photosynthetic protein complexes in thylakoid membrane and discuss the consequences of the light-induced protein network re-organization to the thylakoid membrane ultrastructure.

Cited by 63 publications

References 145 publications

Measuring the dynamic response of the thylakoid architecture in plant leaves by electron microscopy

Measuring the dynamic response of the thylakoid architecture in plant leaves by electron microscopy

PSII Activity Was Inhibited at Flowering Stage with Developing Black Bracts of Oat

Beyond ‘seeing is believing’: the antenna size of the photosystems in vivo

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