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Title: The use of advanced mass spectrometry to dissect the life-cycle of photosystem II

Abstract

Photosystem II (PSII) is a photosynthetic membrane-protein complex that undergoes an intricate, tightly regulated cycle of assembly, damage, and repair. The available crystal structures of cyanobacterial PSII are an essential foundation for understanding PSII function, but nonetheless provide a snapshot only of the active complex. To study aspects of the entire PSII life-cycle, mass spectrometry (MS) has emerged as a powerful tool that can be used in conjunction with biochemical techniques. In this article, we present the MS-based approaches that are used to study PSII composition, dynamics, and structure, and review the information about the PSII life-cycle that has been gained by these methods. This information includes the composition of PSII subcomplexes, discovery of accessory PSII proteins, identification of post-translational modifications and quantification of their changes under various conditions, determination of the binding site of proteins not observed in PSII crystal structures, conformational changes that underlie PSII functions, and identification of water and oxygen channels within PSII. Lastly, we conclude with an outlook for the opportunity of future MS contributions to PSII research.

Authors:
 [1];  [2];  [3]
  1. Washington Univ., St. Louis, St. Louis, MO (United States). Dept. of Biology; Dept. of Chemistry
  2. Washington Univ., St. Louis, St. Louis, MO (United States). Dept. of Chemistry
  3. Washington Univ., St. Louis, St. Louis, MO (United States). Dept. of Biology
Publication Date:
Research Org.:
Washington Univ., St. Louis, MO (United States); Energy Frontier Research Centers (EFRC) (United States). Photosynthetic Antenna Research Center (PARC)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1282178
Grant/Contract Number:  
SC0001035; FG02-99ER20350
Resource Type:
Accepted Manuscript
Journal Name:
Frontiers in Plant Science
Additional Journal Information:
Journal Volume: 7; Journal ID: ISSN 1664-462X
Publisher:
Frontiers Research Foundation
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Photosystem II; Photosystem II life-cycle; mass spectrometry; post-translational modification; chemical cross-linking; protein footprinting; sp pcc 6803; synechocystis sp pcc-6803; cyanobacterium thermosynechococcus-elongatus; manganese-stabilizing protein; integral membrane-proteins; orange carotenoid protein; reaction-center complex; alga chlamydomonas-reinhardtii; excitation-energy distribution

Citation Formats

Weisz, Daniel A., Gross, Michael L., and Pakrasi, Himadri B. The use of advanced mass spectrometry to dissect the life-cycle of photosystem II. United States: N. p., 2016. Web. doi:10.3389/fpls.2016.00617.
Weisz, Daniel A., Gross, Michael L., & Pakrasi, Himadri B. The use of advanced mass spectrometry to dissect the life-cycle of photosystem II. United States. doi:10.3389/fpls.2016.00617.
Weisz, Daniel A., Gross, Michael L., and Pakrasi, Himadri B. Tue . "The use of advanced mass spectrometry to dissect the life-cycle of photosystem II". United States. doi:10.3389/fpls.2016.00617. https://www.osti.gov/servlets/purl/1282178.
@article{osti_1282178,
title = {The use of advanced mass spectrometry to dissect the life-cycle of photosystem II},
author = {Weisz, Daniel A. and Gross, Michael L. and Pakrasi, Himadri B.},
abstractNote = {Photosystem II (PSII) is a photosynthetic membrane-protein complex that undergoes an intricate, tightly regulated cycle of assembly, damage, and repair. The available crystal structures of cyanobacterial PSII are an essential foundation for understanding PSII function, but nonetheless provide a snapshot only of the active complex. To study aspects of the entire PSII life-cycle, mass spectrometry (MS) has emerged as a powerful tool that can be used in conjunction with biochemical techniques. In this article, we present the MS-based approaches that are used to study PSII composition, dynamics, and structure, and review the information about the PSII life-cycle that has been gained by these methods. This information includes the composition of PSII subcomplexes, discovery of accessory PSII proteins, identification of post-translational modifications and quantification of their changes under various conditions, determination of the binding site of proteins not observed in PSII crystal structures, conformational changes that underlie PSII functions, and identification of water and oxygen channels within PSII. Lastly, we conclude with an outlook for the opportunity of future MS contributions to PSII research.},
doi = {10.3389/fpls.2016.00617},
journal = {Frontiers in Plant Science},
number = ,
volume = 7,
place = {United States},
year = {2016},
month = {5}
}

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