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OCPSTRUCTDYNAMICS SIGNED

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

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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.

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

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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