Biochemical and molecular properties of LHCX1, the essential regulator of dynamic photoprotection in diatoms.


Journal

Plant physiology
ISSN: 1532-2548
Titre abrégé: Plant Physiol
Pays: United States
ID NLM: 0401224

Informations de publication

Date de publication:
20 01 2022
Historique:
received: 21 05 2021
accepted: 06 08 2021
pubmed: 2 10 2021
medline: 11 3 2022
entrez: 1 10 2021
Statut: ppublish

Résumé

Light harvesting is regulated by a process triggered by the acidification of the thylakoid lumen, known as nonphotochemical "energy-dependent quenching" (qE). In diatoms, qE is controlled by the light-harvesting complex (LHC) protein LHCX1, while the LHC stress-related (LHCSR) and photosystem II subunit S proteins are essential for green algae and plants, respectively. Here, we report a biochemical and molecular characterization of LHCX1 to investigate its role in qE. We found that, when grown under intermittent light, Phaeodactylum tricornutum forms very large qE, due to LHCX1 constitutive upregulation. This "super qE" is abolished in LHCX1 knockout mutants. Biochemical and spectroscopic analyses of LHCX1 reveal that this protein might differ in the character of binding pigments relative to the major pool of light-harvesting antenna proteins. The possibility of transient pigment binding or not binding pigments at all is discussed. Targeted mutagenesis of putative protonatable residues (D95 and E205) in transgenic P. tricornutum lines does not alter qE capacity, showing that they are not involved in sensing lumen pH, differently from residues conserved in LHCSR3. Our results suggest functional divergence between LHCX1 and LHCSR3 in qE modulation. We propose that LHCX1 evolved independently to facilitate dynamic tracking of light fluctuations in turbulent waters. The evolution of LHCX(-like) proteins in organisms with secondary red plastids, such as diatoms, might have conferred a selective advantage in the control of dynamic photoprotection, ultimately resulting in their ecological success.

Identifiants

pubmed: 34595530
pii: 6365952
doi: 10.1093/plphys/kiab425
pmc: PMC8774712
doi:

Substances chimiques

Light-Harvesting Protein Complexes 0
Photosystem II Protein Complex 0

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

509-525

Informations de copyright

© American Society of Plant Biologists 2021. All rights reserved. For permissions, please email: journals.permissions@oup.com.

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Auteurs

Vasco Giovagnetti (V)

School of Biological and Chemical Sciences, Queen Mary University of London, London E1 4NS, UK.

Marianne Jaubert (M)

Laboratoire de Biologie du Chloroplaste et Perception de la Lumière Chez les Micro-algues, UMR7141, CNRS, Sorbonne Université, Institut de Biologie Physico-Chimique, Paris 75005, France.

Mahendra K Shukla (MK)

School of Biological and Chemical Sciences, Queen Mary University of London, London E1 4NS, UK.

Petra Ungerer (P)

School of Biological and Chemical Sciences, Queen Mary University of London, London E1 4NS, UK.

Jean-Pierre Bouly (JP)

Laboratoire de Biologie du Chloroplaste et Perception de la Lumière Chez les Micro-algues, UMR7141, CNRS, Sorbonne Université, Institut de Biologie Physico-Chimique, Paris 75005, France.

Angela Falciatore (A)

Laboratoire de Biologie du Chloroplaste et Perception de la Lumière Chez les Micro-algues, UMR7141, CNRS, Sorbonne Université, Institut de Biologie Physico-Chimique, Paris 75005, France.

Alexander V Ruban (AV)

School of Biological and Chemical Sciences, Queen Mary University of London, London E1 4NS, UK.

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Classifications MeSH