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The Use of Advanced Mass Spectrometry to Dissect the Life-Cycle of Photosystem II.

Weisz DA, Gross ML, Pakrasi HB - Front Plant Sci (2016)

Bottom Line: 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.We conclude with an outlook for the opportunity of future MS contributions to PSII research.

View Article: PubMed Central - PubMed

Affiliation: Department of Biology, Washington University in St. LouisSt. Louis, MO, USA; Department of Chemistry, Washington University in St. LouisSt. Louis, MO, USA.

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. We conclude with an outlook for the opportunity of future MS contributions to PSII research.

No MeSH data available.


Related in: MedlinePlus

Plot of publications that use MS for PSII research over time. Publications that contain “Photosystem II” and “mass spectrometry” in their article title, abstract, or keywords were searched on the Scopus database. Each data point represents the total number of publications for that range of years.
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Figure 1: Plot of publications that use MS for PSII research over time. Publications that contain “Photosystem II” and “mass spectrometry” in their article title, abstract, or keywords were searched on the Scopus database. Each data point represents the total number of publications for that range of years.

Mentions: These four pillars of proteomics have each become indispensable tools for gleaning information about photosynthesis (Battchikova et al., 2015; Bricker et al., 2015; Heinz et al., 2016) and, in particular for this review, the life-cycle of PSII. A search for publications containing both “Photosystem II” and “mass spectrometry” in the article title, abstract, and/or keywords was performed on the Scopus database. The results, displayed in Figure 1, show that prior to the advent of ESI and MALDI in the late 1980s, publications were nearly zero per year. Starting in the early 1990s and continuing through 2015, publications have risen steadily, with around 20–30 publications per year in the last several years. The rise can be attributed to method and instrument development, and to increasing accessibility of MS instrumentation to biology researchers. An overview of how MS-based tools are typically applied to PSII life-cycle research is given in Table 1. This review focuses on MS of proteins. However, it should be noted that another widely used application of MS in PSII research is the analysis of the isotopic composition of evolved oxygen by membrane-inlet mass spectrometry. This technique has yielded significant insight into the mechanistic aspects of water oxidation by PSII (reviewed in Shevela and Messinger, 2013).


The Use of Advanced Mass Spectrometry to Dissect the Life-Cycle of Photosystem II.

Weisz DA, Gross ML, Pakrasi HB - Front Plant Sci (2016)

Plot of publications that use MS for PSII research over time. Publications that contain “Photosystem II” and “mass spectrometry” in their article title, abstract, or keywords were searched on the Scopus database. Each data point represents the total number of publications for that range of years.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4862242&req=5

Figure 1: Plot of publications that use MS for PSII research over time. Publications that contain “Photosystem II” and “mass spectrometry” in their article title, abstract, or keywords were searched on the Scopus database. Each data point represents the total number of publications for that range of years.
Mentions: These four pillars of proteomics have each become indispensable tools for gleaning information about photosynthesis (Battchikova et al., 2015; Bricker et al., 2015; Heinz et al., 2016) and, in particular for this review, the life-cycle of PSII. A search for publications containing both “Photosystem II” and “mass spectrometry” in the article title, abstract, and/or keywords was performed on the Scopus database. The results, displayed in Figure 1, show that prior to the advent of ESI and MALDI in the late 1980s, publications were nearly zero per year. Starting in the early 1990s and continuing through 2015, publications have risen steadily, with around 20–30 publications per year in the last several years. The rise can be attributed to method and instrument development, and to increasing accessibility of MS instrumentation to biology researchers. An overview of how MS-based tools are typically applied to PSII life-cycle research is given in Table 1. This review focuses on MS of proteins. However, it should be noted that another widely used application of MS in PSII research is the analysis of the isotopic composition of evolved oxygen by membrane-inlet mass spectrometry. This technique has yielded significant insight into the mechanistic aspects of water oxidation by PSII (reviewed in Shevela and Messinger, 2013).

Bottom Line: 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.We conclude with an outlook for the opportunity of future MS contributions to PSII research.

View Article: PubMed Central - PubMed

Affiliation: Department of Biology, Washington University in St. LouisSt. Louis, MO, USA; Department of Chemistry, Washington University in St. LouisSt. Louis, MO, USA.

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. We conclude with an outlook for the opportunity of future MS contributions to PSII research.

No MeSH data available.


Related in: MedlinePlus