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Adjélé Wilson
Université Paris-Saclay
9Publications
5H-index
67Citations
Publications 9
Newest
#1Fernando Muzzopappa (Université Paris-Saclay)H-Index: 3
#2Adjélé Wilson (Université Paris-Saclay)H-Index: 5
Last.Diana Kirilovsky (Université Paris-Saclay)H-Index: 9
view all 3 authors...
The photoactive orange carotenoid protein (OCP) is a blue-light intensity sensor involved in cyanobacterial photoprotection. Three OCP families co-exist (OCPX, OCP1 and OCP2), having originated from the fusion of ancestral domain genes. Here, we report the characterization of an OCPX and the evolutionary characterization of OCP paralogues focusing on the role of the linker connecting the domains. The addition of the linker with specific amino acids enabled the photocycle of the OCP ancestor. OCP...
#1Yury B. Slonimskiy (MSU: Moscow State University)H-Index: 6
#2Fernando Muzzopappa (Université Paris-Saclay)H-Index: 3
Last.Nikolai N. Sluchanko (MSU: Moscow State University)H-Index: 18
view all 7 authors...
Carotenoids are lipophilic pigments with multiple biological functions from coloration to vision and photoprotection. Still, the number of water-soluble carotenoid-binding proteins described to date is limited, and carotenoid transport and carotenoprotein maturation processes are largely underexplored. Recent studies revealed that CTDHs, which are natural homologs of the C-terminal domain (CTD) of the Orange Carotenoid Protein (OCP), a photoswitch involved in cyanobacterial photoprotection, are ...
#1Alberto Mezzetti (University of Paris)H-Index: 14
#2Maxime T. A. Alexandre (Université Paris-Saclay)H-Index: 14
Last.Diana Kirilovsky (Université Paris-Saclay)H-Index: 9
view all 6 authors...
The orange carotenoid protein (OCP), which is essential in cyanobacterial photoprotection, is the first photoactive protein containing a carotenoid as an active chromophore. Static and time-resolved Fourier transform infrared (FTIR) difference spectroscopy under continuous illumination at different temperatures was applied to investigate its photoactivation mechanism. Here, we demonstrate that in the OCP, the photo-induced conformational change involves at least two different steps, both in the ...
#1Patrick E. Konold (VU: VU University Amsterdam)H-Index: 4
#2I.H.M. van Stokkum (VU: VU University Amsterdam)H-Index: 58
Last.John T. M. Kennis (VU: VU University Amsterdam)H-Index: 38
view all 7 authors...
The orange carotenoid protein (OCP) is a two-domain photoactive protein that noncovalently binds an echinenone (ECN) carotenoid and mediates photoprotection in cyanobacteria. In the dark, OCP assumes an orange, inactive state known as OCPO; blue light illumination results in the red active state, known as OCPR. The OCPR state is characterized by large-scale structural changes that involve dissociation and separation of C-terminal and N-terminal domains accompanied by carotenoid translocation int...
#1Alberto MezzettiH-Index: 14
Last.Diana KirilovskyH-Index: 1
view all 6 authors...
The Orange Carotenoid Protein (OCP), which is essential in cyanobacterial photoprotection, is the first photoactive protein containing a carotenoid as an active chromophore. Static and time-resolved FTIR difference spectroscopy under continuous illumination at different temperatures was applied to investigate its photoactivation mechanism. Here we demonstrate that in the OCP, the photo-induced conformational change involves at least two different steps, both in the second timescale at 277 K. Eac...
#1Dvir Harris (Technion – Israel Institute of Technology)H-Index: 4
#2Adjélé Wilson (Université Paris-Saclay)H-Index: 5
Last.Noam Adir (Technion – Israel Institute of Technology)H-Index: 30
view all 8 authors...
A recently reported family of soluble cyanobacterial carotenoproteins, homologs of the C-terminal domain (CTDH) of the photoprotective Orange Carotenoid Protein, is suggested to mediate carotenoid transfer from the thylakoid membrane to the Helical Carotenoid Proteins, which are paralogs of the N-terminal domain of the OCP. Here we present the three-dimensional structure of a carotenoid-free CTDH variant from Anabaena (Nostoc) PCC 7120. This CTDH contains a cysteine residue at position 103. Two ...
#1Adrien Thurotte (Université Paris-Saclay)H-Index: 1
#2Céline Bourcier de Carbon (CEA: French Alternative Energies and Atomic Energy Commission)H-Index: 1
Last.Diana Kirilovsky (Université Paris-Saclay)H-Index: 9
view all 7 authors...
Abstract To deal with fluctuating light condition, cyanobacteria have developed a photoprotective mechanism which, under high light conditions, decreases the energy arriving at the photochemical centers. It relies on a photoswitch, the Orange Carotenoid Protein (OCP). Once photoactivated, OCP binds to the light harvesting antenna, the phycobilisome (PBS), and triggers the thermal dissipation of the excess energy absorbed. Deactivation of the photoprotective mechanism requires the intervention of...
#1Václav Šlouf (Sewanee: The University of the South)H-Index: 9
#2Valentyna Kuznetsova (Sewanee: The University of the South)H-Index: 3
Last.Tomáš Polívka (Sewanee: The University of the South)H-Index: 37
view all 7 authors...
A quenching mechanism mediated by the orange carotenoid protein (OCP) is one of the ways cyanobacteria protect themselves against photooxidative stress. Here, we present a femtosecond spectroscopic study comparing OCP and RCP (red carotenoid protein) samples binding different carotenoids. We confirmed significant changes in carotenoid configuration upon OCP activation reported by Leverenz et al. (Science 348:1463–1466. doi: 10.1126/science.aaa7234, 2015) by comparing the transient spectra of OCP...
#1Matthew R. Melnicki (University of California, Berkeley)H-Index: 14
#2Ryan L. Leverenz (MSU: Michigan State University)H-Index: 9
Last.Cheryl A. Kerfeld (MSU: Michigan State University)H-Index: 47
view all 9 authors...
Abstract Using a phylogenomic approach, we have identified and subclassified a new family of carotenoid-binding proteins. These proteins have sequence homology to the N-terminal domain (NTD) of the Orange Carotenoid Protein (OCP), and are referred to as Helical Carotenoid Proteins (HCPs). These proteins comprise at least nine distinct clades and are found in diverse organisms, frequently as multiple paralogs representing the distinct clades. These seem to be out-paralogs maintained from ancient ...
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