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

Abstract

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 themore » 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.« less

Authors:

Weisz, Daniel A. ^[1]; Johnson, Virginia M. ^[1]; Niedzwiedzki, Dariusz M.  ^[2];

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Shinn, Min Kyung ^[3]; Liu, Haijun  ^[1];

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Klitzke, Clécio F. ^[4]; Gross, Michael L.  ^[4];

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Blankenship, Robert E. ^[1]; Lohman, Timothy M. ^[5]; Pakrasi, Himadri B.  ^[1]

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• Search DOE PAGES for ORCID "0000-0001-8240-2123"
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+ Show Author Affiliations

1. Department of Biology, Washington University in St. Louis, St. Louis, MO 63130,
2. Center for Solar Energy &, Energy Storage, Department of Energy, Environmental, &, Chemical Engineering, Washington University in St. Louis, St. Louis, MO 63130,
3. 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,
4. Department of Chemistry, Washington University in St. Louis, St. Louis, MO 63130
5. Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110,

Publication Date:

2019-10-08

Research Org.:

Washington Univ., St. Louis, MO (United States)

Sponsoring Org.:

USDOE; USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division; National Institutes of Health (NIH)

OSTI Identifier:

1571354

Alternate Identifier(s):

OSTI ID: 1800966

Grant/Contract Number:  

FG02-99ER20350; SC 0001035; SC0001035; P41GM103422; GM030498; T32 EB014855

Resource Type:

Published Article

Journal Name:

Proceedings of the National Academy of Sciences of the United States of America

Additional Journal Information:

Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Volume: 116 Journal Issue: 43; Journal ID: ISSN 0027-8424

Publisher:

Proceedings of the National Academy of Sciences

Country of Publication:

United States

Language:

English

Subject:

59 BASIC BIOLOGICAL SCIENCES; photosynthesis; repair cycle; protein turnover; mass spectrometry; ultrafast; spectroscopy