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OCPSTRUCTDYNAMICS SIGNED

Structural dynamics essential for photosynthetic adaptation and survival of cyanobacteria in fluctuating light intensities

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EC-Contrib. €

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 OCPSTRUCTDYNAMICS project word cloud

Explore the words cloud of the OCPSTRUCTDYNAMICS project. It provides you a very rough idea of what is the project "OCPSTRUCTDYNAMICS" about.

light    additional    vulnerable    photo    resolved    slr1963    energy    spectroscopic    carotenoid    subfamilies    cyanobacterial    ocp1    transitions    gene    encoded    cyanobacteria    photochemical    domains    synechocystis    diffraction    crystallography    performed    spectroscopy    exact    resolve    photosynthesis    biofuel    harvesting    triggered    proteins    photoprotection    activation    protect    npq    absorption    orange    polarised    paralogs    ray    quenching    flow    interactions    terminal    protein    mechanisms    transient    excess    photosynthetic    optogenetics    identification    demonstrating    roles    structural    suggested    photoprotective    ranging    unravelled    absorbed    damage    artificial    photoenergy    fluctuations    raised    organisms    isolated    genomes    dissipation    dynamics    like    describe    movement    dissociation    machinery    ultrafast    differences    questions    causing    themselves    ocpx    intensity    single    allowed    date    oriented    heat    crystals    time    mechanism    first    ocp2    structure    occurs    ocp    kinetics    dependent    combined    photoactivation    6803   

Project "OCPSTRUCTDYNAMICS" data sheet

The following table provides information about the project.

Coordinator
IMPERIAL COLLEGE OF SCIENCE TECHNOLOGY AND MEDICINE 

Organization address
address: SOUTH KENSINGTON CAMPUS EXHIBITION ROAD
city: LONDON
postcode: SW7 2AZ
website: http://www.imperial.ac.uk/

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country United Kingdom [UK]
 Total cost 212˙933 €
 EC max contribution 212˙933 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2018
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2020
 Duration (year-month-day) from 2020-01-08   to  2022-01-07

 Partnership

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# participants  country  role  EC contrib. [€] 
1    IMPERIAL COLLEGE OF SCIENCE TECHNOLOGY AND MEDICINE UK (LONDON) coordinator 212˙933.00

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 Project objective

Like most photosynthetic organisms, cyanobacteria are vulnerable to fluctuations in light intensity, which can damage their photosynthetic machinery. To protect themselves against such fluctuations, they use a photoprotective mechanism called non-photochemical quenching (NPQ), i.e. the dissipation of excess absorbed photo-energy as heat. NPQ in cyanobacteria is triggered by orange carotenoid protein (OCP) light activation. Based on spectroscopic and diffraction studies of OCP in Synechocystis 6803 (gene slr1963), it was suggested that OCP light activation occurs through light-induced movement of a carotenoid causing movement and/or dissociation of OCP N- and C-terminal domains. However, the exact structural dynamics of OCP light-activation need to be unravelled. Furthermore, the growing availability of cyanobacterial genomes allowed identification of additional OCP subfamilies (OCP2, OCPX) in different cyanobacteria. The first results demonstrating different kinetics of light-activation in the different OCP paralogs raised questions about differences in their photoprotective roles and in photoactivation mechanisms. This topic has not been studied to date. Here I propose to resolve structural changes during photoprotection-related transitions of OCP in different OCP subfamilies using time-resolved X-ray crystallography. X-ray crystallography of OCP1 encoded by slr1963, the best-characterized OCP protein, as well as its paralogs from the OCP2 and OCPX subfamilies will be performed. This approach will be combined with ultrafast transient (polarised) absorption spectroscopy on isolated proteins and oriented single crystals to describe the structure-dependent flow of photoenergy in the proteins. This study has several potential applications ranging from enhancing cyanobacterial light harvesting to improve biofuel production, to better understanding of carotenoid-protein interactions in artificial photosynthesis systems, and for optogenetics.

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