Heterologous Expression of Moss Light-harvesting Complex Stress-related 1 (LHCSR1), the Chlorophyll a-Xanthophyll Pigment-protein Complex Catalyzing Non-photochemical Quenching, in Nicotiana sp.

Pinnola, Alberta; Ghin, Leonardo; Gecchele, Elisa; Merlin, Matilde; Alboresi, Alessandro; Avesani, Linda; Pezzotti, Mario; Capaldi, Stefano; Cazzaniga, Stefano; Bassi, Roberto

doi:10.1074/jbc.m115.668798

Cited by 27 publications

(30 citation statements)

References 61 publications

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“…Some Chl b disconnections (most likely due to lose binding of this Chl type to LHCSR3 [20,36]) are indeed observed in the sample (Fig. S1) as observed previously [20].…”

Section: Energy Transfer Within Lhcsr3supporting

confidence: 80%

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Excitation dynamics and structural implication of the stress-related complex LHCSR3 from the green alga Chlamydomonas reinhardtii

Liguori

Novoderezhkin

Roy

et al. 2016

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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LHCSR3 is a member of the Light-Harvesting Complexes (LHC) family, which is mainly composed of pigment-protein complexes responsible for collecting photons during the first steps of photosynthesis. Unlike related LHCs, LHCSR3 is expressed in stress conditions and has been shown to be essential for the fast component of photoprotection, non-photochemical quenching (NPQ), in the green alga Chlamydomonas reinhardtii. In plants, which do not possess LHCSR homologs, NPQ is triggered by the PSBS protein. Both PSBS and LHCSR3 possess the ability to sense pH changes but, unlike PSBS, LHCSR3 binds multiple pigments. In this work we have analyzed the properties of the pigments bound to LHCSR3 and their excited state dynamics. The data show efficient excitation energy transfer between pigments with rates similar to those observed for the other LHCs. Application of an exciton model based on a template of LHCII, the most abundant LHC, satisfactorily explains the collected steady state and time-resolved spectroscopic data, indicating that LHCSR3 has a LHC-like molecular architecture, although it probably binds less pigments. The model suggests that most of the chlorophylls have similar energy and interactions as in LHCII. The most striking difference is the localization of the lowest energy state, which is not on the Chlorophyll a (Chl a) 610-611-612 triplet as in all the LHCB antennas, but on Chl a613, which is located close to the lumen and to the pH-sensing region of the protein.

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“…Some Chl b disconnections (most likely due to lose binding of this Chl type to LHCSR3 [20,36]) are indeed observed in the sample (Fig. S1) as observed previously [20].…”

Section: Energy Transfer Within Lhcsr3supporting

confidence: 80%

“…The Chl a/b ratio (5.5) of LHCSR3 was significantly higher than that of LHCII (Lhcb1.3 [22]) or related LHCs for which values varying between~1 (CP24) [34] and 3.0 (CP29) [35] have been reported. This indicates a higher bindingaffinity for Chl a, as reported also for the homologous LHCSR from mosses [36].…”

Section: Pigment-binding Properties Of Lhcsr3supporting

confidence: 79%

Excitation dynamics and structural implication of the stress-related complex LHCSR3 from the green alga Chlamydomonas reinhardtii

Liguori

Novoderezhkin

Roy

et al. 2016

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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“…Under high light (sunny), LHCs also dissipate excess energy as heat through a process known as nonphotochemical quenching (NPQ), which is activated by conformational changes (14,15). In unicellular algae and mosses, Light-Harvesting Complex Stress Related 1 (LHCSR1) is the LHC responsible for dissipation (16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27). Single-molecule spectroscopy of LHCSR1 revealed frequent transitions between bright (photoactive) and dim (quenched) states (9).…”

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confidence: 99%

Microsecond and millisecond dynamics in the photosynthetic protein LHCSR1 observed by single-molecule correlation spectroscopy

Kondô

Gordon

Pinnola

et al. 2019

Proc. Natl. Acad. Sci. U.S.A.

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Biological systems are subjected to continuous environmental fluctuations, and therefore, flexibility in the structure and function of their protein building blocks is essential for survival. Protein dynamics are often local conformational changes, which allows multiple dynamical processes to occur simultaneously and rapidly in individual proteins. Experiments often average over these dynamics and their multiplicity, preventing identification of the molecular origin and impact on biological function. Green plants survive under high light by quenching excess energy, and Light-Harvesting Complex Stress Related 1 (LHCSR1) is the protein responsible for quenching in moss. Here, we expand an analysis of the correlation function of the fluorescence lifetime by improving the estimation of the lifetime states and by developing a multicomponent model correlation function, and we apply this analysis at the single-molecule level. Through these advances, we resolve previously hidden rapid dynamics, including multiple parallel processes. By applying this technique to LHCSR1, we identify and quantitate parallel dynamics on hundreds of microseconds and tens of milliseconds timescales, likely at two quenching sites within the protein. These sites are individually controlled in response to fluctuations in sunlight, which provides robust regulation of the light-harvesting machinery. Considering our results in combination with previous structural, spectroscopic, and computational data, we propose specific pigments that serve as the quenching sites. These findings, therefore, provide a mechanistic basis for quenching, illustrating the ability of this method to uncover protein function.single-molecule fluorescence spectroscopy | photosynthetic light harvesting | nonphotochemical quenching | protein dynamics

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“…To determine if the LHCII composition between LL‐ and HL‐acclimated cells was different, we excised B9 and identified tryptic peptides using mass spectroscopy (Table ), showing that B9 from HL contained an additional component, identified as LhcSR1, that was absent in LL samples. Spectroscopic analysis of lhcsr family proteins has shown a distinctive red‐shift in absorbance and fluorescence properties (Bonente et al ., ; Pinnola et al ., ), and we therefore assign the red‐shifted emission spectrum in HL samples to the expression and association of LhcSR1 with the trimers.…”

Section: Resultsmentioning

confidence: 99%

Spectroanalysis in native gels (SING): rapid spectral analysis of pigmented thylakoid membrane complexes separated by CN–PAGE

et al. 2017

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Photosynthetic organisms rapidly adjust the capture, transfer and utilization of light energy to optimize the efficiency of photosynthesis and avoid photodamage. These adjustments involve fine-tuning of expression levels and mutual interactions among electron/proton transfer components and their associated light-harvesting antenna. Detailed studies of these interactions and their dynamics have been hindered by the low throughput and resolution of currently available research tools, which involve laborious isolation, separation and characterization steps. To address these issues, we developed an approach that measured multiple spectroscopic properties of thylakoid preparations directly in native polyacrylamide gel electrophoresis gels, enabling unprecedented resolution of photosynthetic complexes, both in terms of the spectroscopic and functional details, as well as the ability to distinguish separate complexes and thus test their functional connections. As a demonstration, we explore the thylakoid membrane components of Chlamydomonas reinhardtii acclimated to high and low light, using a combination of room temperature absorption and 77K fluorescence emission to generate a multi-dimensional molecular and spectroscopic map of the photosynthetic apparatus. We show that low-light-acclimated cells accumulate a photosystem I-containing megacomplex that is absent in high-light-acclimated cells and contains distinct LhcII proteins that can be distinguished based on their spectral signatures.

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Heterologous Expression of Moss Light-harvesting Complex Stress-related 1 (LHCSR1), the Chlorophyll a-Xanthophyll Pigment-protein Complex Catalyzing Non-photochemical Quenching, in Nicotiana sp.

Cited by 27 publications

References 61 publications

Excitation dynamics and structural implication of the stress-related complex LHCSR3 from the green alga Chlamydomonas reinhardtii

Excitation dynamics and structural implication of the stress-related complex LHCSR3 from the green alga Chlamydomonas reinhardtii

Microsecond and millisecond dynamics in the photosynthetic protein LHCSR1 observed by single-molecule correlation spectroscopy

Spectroanalysis in native gels (SING): rapid spectral analysis of pigmented thylakoid membrane complexes separated by CN–PAGE

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