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:
-
- Washington Univ., St. Louis, St. Louis, MO (United States). Dept. of Biology; Dept. of Chemistry
- Washington Univ., St. Louis, St. Louis, MO (United States). Dept. of Chemistry
- 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)
- 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. https://doi.org/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. https://doi.org/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 = {Tue May 10 00:00:00 EDT 2016},
month = {Tue May 10 00:00:00 EDT 2016}
}
Web of Science
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Works referencing / citing this record:
Mass spectrometry-based cross-linking study shows that the Psb28 protein binds to cytochrome b 559 in Photosystem II
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