A novel chlorophyll protein complex in the repair cycle of photosystem II.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
22 10 2019
Historique:
pubmed: 9 10 2019
medline: 3 4 2020
entrez: 10 10 2019
Statut: ppublish

Résumé

In oxygenic photosynthetic organisms, photosystem II (PSII) is a unique membrane protein complex that catalyzes light-driven oxidation of water. PSII undergoes frequent damage due to its demanding photochemistry. It must undergo a repair and reassembly process following photodamage, many facets of which remain unknown. We have discovered a PSII subcomplex that lacks 5 key PSII core reaction center polypeptides: D1, D2, PsbE, PsbF, and PsbI. This pigment-protein complex does contain the PSII core antenna proteins CP47 and CP43, as well as most of their associated low molecular mass subunits, and the assembly factor Psb27. Immunoblotting, mass spectrometry, and ultrafast spectroscopic results support the absence of a functional reaction center in this complex, which we call the "no reaction center" complex (NRC). Analytical ultracentrifugation and clear native PAGE analysis show that NRC is a stable pigment-protein complex and not a mixture of free CP47 and CP43 proteins. NRC appears in higher abundance in cells exposed to high light and impaired protein synthesis, and genetic deletion of PsbO on the PSII luminal side results in an increased NRC population, indicative that NRC forms in response to photodamage as part of the PSII repair process. Our finding challenges the current model of the PSII repair cycle and implies an alternative PSII repair strategy. Formation of this complex may maximize PSII repair economy by preserving intact PSII core antennas in a single complex available for PSII reassembly, minimizing the risk of randomly diluting multiple recycling components in the thylakoid membrane following a photodamage event.

Identifiants

pubmed: 31594847
pii: 1909644116
doi: 10.1073/pnas.1909644116
pmc: PMC6815111
doi:

Substances chimiques

Photosystem II Protein Complex 0
Chlorophyll 1406-65-1

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

21907-21913

Subventions

Organisme : NIGMS NIH HHS
ID : P41 GM103422
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM030498
Pays : United States
Organisme : NIBIB NIH HHS
ID : T32 EB014855
Pays : United States

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

Daniel A Weisz (DA)

Department of Biology, Washington University in St. Louis, St. Louis, MO 63130.

Virginia M Johnson (VM)

Department of Biology, Washington University in St. Louis, St. Louis, MO 63130.

Dariusz M Niedzwiedzki (DM)

Center for Solar Energy & Energy Storage, Department of Energy, Environmental, & Chemical Engineering, Washington University in St. Louis, St. Louis, MO 63130.

Min Kyung Shinn (MK)

Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110.
Department of Physics, Washington University in St. Louis, St. Louis, MO 63130.

Haijun Liu (H)

Department of Biology, Washington University in St. Louis, St. Louis, MO 63130.

Clécio F Klitzke (CF)

Department of Chemistry, Washington University in St. Louis, St. Louis, MO 63130.

Michael L Gross (ML)

Department of Chemistry, Washington University in St. Louis, St. Louis, MO 63130.

Robert E Blankenship (RE)

Department of Biology, Washington University in St. Louis, St. Louis, MO 63130.

Timothy M Lohman (TM)

Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110.

Himadri B Pakrasi (HB)

Department of Biology, Washington University in St. Louis, St. Louis, MO 63130; Pakrasi@wustl.edu.

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Classifications MeSH