Dataset Information

Light acclimation response of the thylakoid proteome in Arabidopsis

ABSTRACT: The plant chloroplast thylakoid membrane must respond to environmental variations in light intensity to maximise the efficiency of photosynthesis and minimise photo-oxidative stress. Plants respond to changing light intensity in the short-term (seconds to minutes) through altered regulation of the structure and function of existing thylakoid components, whereas long-term acclimation (hours to days) involves changes in gene expression, protein synthesis and degradation, which modulate the composition of the thylakoid membrane. Here we have investigated the long-term changes in the thylakoid membrane composition in Arabidopsis thaliana plants acclimated to low, moderate and high light intensities using quantitative label-free proteomics in combination with a range of biochemical and spectroscopic functional analyses.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell

DISEASE(S): Disease Free

SUBMITTER: Sarah Flannery

LAB HEAD: Matthew P Johnson

PROVIDER: PXD014982 | Pride | 2021-08-23

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	20181130_SF_Ara_SL_150a1-023.raw	Raw
	20181130_SF_Ara_SL_150a2-017.raw	Raw
	20181130_SF_Ara_SL_150a3-012.raw	Raw
	20181130_SF_Ara_SL_150b1-015.raw	Raw
	20181130_SF_Ara_SL_150b2-004.raw	Raw

Items per page:

1 - 5 of 29

Publications

Developmental acclimation of the thylakoid proteome to light intensity in Arabidopsis.

Flannery Sarah E SE Hepworth Christopher C Wood William H J WHJ Pastorelli Federica F Hunter Christopher N CN Dickman Mark J MJ Jackson Philip J PJ Johnson Matthew P MP

The Plant journal : for cell and molecular biology 20201127 1

Photosynthetic acclimation, the ability to adjust the composition of the thylakoid membrane to optimise the efficiency of electron transfer to the prevailing light conditions, is crucial to plant fitness in the field. While much is known about photosynthetic acclimation in Arabidopsis, to date there has been no study that combines both quantitative label-free proteomics and photosynthetic analysis by gas exchange, chlorophyll fluorescence and P700 absorption spectroscopy. Using these methods we ...[more]

PMID: 33118270

Similar Datasets

Project description:The regulation of the photosynthetic apparatus in higher plants is highly connected to the organization of the thylakoid membrane into appressed and non-appressed regions. The two photosystems (I and II) are the spatially strongest segregated protein complexes by this thylakoid heterogenous organization, with PSII predominantly present in the appressed membranes (grana), while PSI is confined to the stroma-exposed non-appressed thylakoid membranes (lamellae). Stacking of thylakoid membranes in grana is highly dynamic and influenced by the levels of PSII and LHCII protein phosphorylation which, in turn, are dependent on changes in light intensity and quality and thus, ultimately, on the redox state of the electron transfer chain. Dynamics of this lateral heterogeneity controls the spillover of excitation energy from PSII to PSI and optimizes the photochemistry in constantly fluctuating light conditions. Recently, a family of membrane-integral thylakoid proteins named CURVATURE THYLAKOID 1 (CURT1) have been proposed as new key components in shaping both the width and the number of layers per granum in response to changes in light intensity. CURT1B, in particular, has been known for a long time as a relatively abundant phosphorylated and acetylated protein, but so far the role and dynamics of these post-translational modifications (PTMs) have not been revealed. To this end, we have quantified by means of targeted proteomics the amount of CURT1 proteins and the level of CURT1B PTMs after short-term fluctuating light treatments in wild type Arabidopsis thaliana and the knock-out mutants of the kinases STN7 and STN8 and of the phosphatase TAP38. The CURT1B protein was first localized to a specific curvature domain largely depleted of the chlorophyll-protein complexes. Moreover, we have found that CURT1B is either phosphorylated or acetylated in the N-terminus, but never both. While the level of acetylation is never affected by the light treatments, the phosphorylation increases in light conditions that lead to sudden increase in PSII core protein phosphorylation, and these dynamics are largely abolished in stn8 plants but not in stn7 or tap38. Intriguingly, the phosphorylation dynamics as well as the level of the other CURT1 proteins, are instead highly affected in psb33 plants, which lack LHCII phosphorylation dynamics, and in the psal plants, which show constitutively phosphorylated LHCII. These results provide important information for assessing the relationships between PSII-LHCII phosphorylation, CURT1B phosphorylation and the dynamics of the appressed thylakoids, which in turn allow optimal photosynthesis and provide photoprotection under fluctuations in light intensity.