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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.

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

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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