Oligomerization processes limit photoactivation and recovery of the orange carotenoid protein.


Journal

Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626

Informations de publication

Date de publication:
02 08 2022
Historique:
received: 04 02 2022
revised: 17 05 2022
accepted: 01 07 2022
pubmed: 8 7 2022
medline: 6 8 2022
entrez: 7 7 2022
Statut: ppublish

Résumé

The orange carotenoid protein (OCP) is a photoactive protein involved in cyanobacterial photoprotection by quenching of the excess of light-harvested energy. The photoactivation mechanism remains elusive, in part due to absence of data pertaining to the timescales over which protein structural changes take place. It also remains unclear whether or not oligomerization of the dark-adapted and light-adapted OCP could play a role in the regulation of its energy-quenching activity. Here, we probed photoinduced structural changes in OCP by a combination of static and time-resolved X-ray scattering and steady-state and transient optical spectroscopy in the visible range. Our results suggest that oligomerization partakes in regulation of the OCP photocycle, with different oligomers slowing down the overall thermal recovery of the dark-adapted state of OCP. They furthermore reveal that upon non-photoproductive excitation a numbed state forms, which remains in a non-photoexcitable structural state for at least ≈0.5 μs after absorption of a first photon.

Identifiants

pubmed: 35794830
pii: S0006-3495(22)00550-1
doi: 10.1016/j.bpj.2022.07.004
pmc: PMC9388578
pii:
doi:

Substances chimiques

Bacterial Proteins 0
Carotenoids 36-88-4

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

2849-2872

Informations de copyright

Copyright © 2022 Biophysical Society. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests.

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Auteurs

Elena A Andreeva (EA)

Institut de Biologie Structurale (IBS), Université Grenoble Alpes, CEA, CNRS, Grenoble, France; Max-Planck-Institut für medizinische Forschung, Heidelberg, Germany.

Stanisław Niziński (S)

Quantum Electronics Laboratory, Faculty of Physics, Adam Mickiewicz University in Poznan, Poznan, Poland; Univ. Lille, CNRS, UMR 8516 - LASIRe - Laboratoire de Spectroscopie pour les Interactions la Réactivité et l'Environnement, F-59000 Lille, France.

Adjélé Wilson (A)

Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette, France.

Matteo Levantino (M)

European Synchrotron Radiation Facility (ESRF), Grenoble, France.

Elke De Zitter (E)

Institut de Biologie Structurale (IBS), Université Grenoble Alpes, CEA, CNRS, Grenoble, France.

Rory Munro (R)

Institut de Biologie Structurale (IBS), Université Grenoble Alpes, CEA, CNRS, Grenoble, France.

Fernando Muzzopappa (F)

Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette, France.

Aurélien Thureau (A)

Synchrotron SOLEIL, 91190, Saint Aubin, France.

Ninon Zala (N)

Institut de Biologie Structurale (IBS), Université Grenoble Alpes, CEA, CNRS, Grenoble, France.

Gotard Burdzinski (G)

Quantum Electronics Laboratory, Faculty of Physics, Adam Mickiewicz University in Poznan, Poznan, Poland.

Michel Sliwa (M)

Univ. Lille, CNRS, UMR 8516 - LASIRe - Laboratoire de Spectroscopie pour les Interactions la Réactivité et l'Environnement, F-59000 Lille, France.

Diana Kirilovsky (D)

Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette, France.

Giorgio Schirò (G)

Institut de Biologie Structurale (IBS), Université Grenoble Alpes, CEA, CNRS, Grenoble, France.

Jacques-Philippe Colletier (JP)

Institut de Biologie Structurale (IBS), Université Grenoble Alpes, CEA, CNRS, Grenoble, France. Electronic address: colletier@ibs.fr.

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