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Proteomic Analysis of the Photosystem I Light-Harvesting Antenna in Tomato (Lycopersicon esculentum)†

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Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, Institut für Allgemeine Botanik, Johannes Gutenberg-Universität Mainz, Müllerweg 6, 55099 Mainz, Germany, and Lehrstuhl für Pflanzenphysiologie, Friedrich Schiller-Universität Jena, Dornburger Strasse 159, 07743 Jena, Germany
Cite this: Biochemistry 2004, 43, 28, 9214–9224
Publication Date (Web):June 26, 2004
https://doi.org/10.1021/bi0498196
Copyright © 2004 American Chemical Society
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    Abstract

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    Until now, more genes of the light-harvesting antenna of higher-plant photosystem I (PSI) than proteins have been described. To improve our understanding of the composition of light-harvesting complex I (LHCI) of tomato (Lycopersicon esculentum), we combined one- and two-dimensional (1-D and 2-D, respectively) gel electrophoresis with immunoblotting and tandem mass spectrometry (MS/MS). Separation of PSI with high-resolution 1-D gels allowed separation of five bands attributed to proteins of LHCI. Immunoblotting with monospecific antibodies and MS/MS analysis enabled the correct assignment of the four prominent bands to light-harvesting proteins Lhca1−4. The fifth band was recognized by only the Lhca1 antibody. Immunodetection as well as mass spectrometric analysis revealed that these protein bands contain not only the eponymous protein but also other Lhca proteins, indicating a heterogeneous protein composition of Lhca bands. Additionally, highly sensitive MS/MS allowed detection of a second Lhca4 isoform and of Lhca5. These proteins had not been described before on the protein level in higher plants. Two-dimensional gel electrophoresis revealed an even more diverse composition of individual Lhca proteins than was apparent from 1-D gels. For each of the four prominent Lhca proteins, four to five isoforms with different isoelectric points could be identified. In the case of Lhca1, Lhca4, and Lhca3, additional isoforms with slightly differing molecular masses were identified. Thus, we were able to detect four to ten isoforms of each individual Lhca protein in PSI. Reasons for the origin of Lhca heterogeneity are discussed. The observed variety of Lhca proteins and their isoforms is of particular interest in the context of the recently published crystal structure of photosystem I from pea, which showed the presence of only four Lhca proteins per photosystem I. These findings indicate that several populations of photosystem I that differ in their Lhca composition may exist.

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    †

     This project was supported by Grant “Nachwuchsgruppe Pflanzenphysiologie” from the federal state of Thüringen (to M.H.) and Grants Schm 1203/2-3 and 1203/2-4 (to V.H.R.S.) from the Deutsche Forschungsgemeinschaft.

    ‡

     Johannes Gutenberg-Universität Mainz.

    §

     Friedrich Schiller-Universität Jena.

    *

     To whom correspondence should be addressed. M.H.:  phone, 001-215-898-4974; fax, 001-215-898-8780; e-mail, [email protected]. V.H.R.S.:  phone, 0049-6131-3924203; fax, 0049-6131-3923787; e-mail, [email protected].

    ‖

     University of Pennsylvania.

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    25. Zhenle Yang, Xinhua Su, Feng Wu, Yandao Gong, Tingyun Kuang. Effect of phosphatidylglycerol on molecular organization of photosystem I. Biophysical Chemistry 2005, 115 (1) , 19-27. https://doi.org/10.1016/j.bpc.2005.01.004
    26. Stefanie Storf, Stefan Jansson, Volkmar H.R. Schmid. Pigment Binding, Fluorescence Properties, and Oligomerization Behavior of Lhca5, a Novel Light-harvesting Protein. Journal of Biological Chemistry 2005, 280 (7) , 5163-5168. https://doi.org/10.1074/jbc.M411248200
    27. Jon Nield, Kevin Redding, Michael Hippler. Remodeling of Light-Harvesting Protein Complexes in Chlamydomonas in Response to Environmental Changes. Eukaryotic Cell 2004, 3 (6) , 1370-1380. https://doi.org/10.1128/EC.3.6.1370-1380.2004
    28. Nathan Nelson, Adam Ben-Shem. The complex architecture of oxygenic photosynthesis. Nature Reviews Molecular Cell Biology 2004, 5 (12) , 971-982. https://doi.org/10.1038/nrm1525
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