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In Vivo Phosphorylation Site Mapping and Functional Characterization of Arabidopsis Phototropin 1

Molecular Plant 2008年第1期1卷 178-194页

作者： Stuart Sullivan Catriona E. Thomson Douglas J. Lamont Matthew A. Jones John M. Christie Plant Science Group Division of Biochemistry and Molecular Biology. Institute of Biomedical and Life Sciences University of Glasgow. University Avenue. Glasgow Scotland UK FingerPrints Proteomics Facility Post-Genomics and Molecular Interactions Centre. School of Life Sciences MSI/WTB/CIR Complex University of Dundee. Dundee Scotland UK

Phototropins （phot1 and phot2） are blue-light receptor kinases controlling a range of responses that optimize the photosynthetic efficiency of plants. Light sensing is mediated by two flavin-binding motifs, known as LOVl and LOV2, located within the N-terminal region of the protein. Photoexcitation via LOV2 leads to activation of the C-terminal kinase domain and consequently receptor autophosphorylation. However, knowledge of the in-vivo phosphorylation sites for Arabidopsis phototropins is lacking and has impeded progress in elucidating the functional significance of receptor phos- phorylation. We have purified photl from Arabidopsis and identified the in-vivo sites of receptor phosphorylation by liquid chromatography tandem mass spectrometry. Arabidopsis-derived photl binds flavin mononucleotide as chromophore and is phosphorylated at four major sites located upstream of LOV2 （Ser^58, Ser^85, Ser^350, and Ser^410）, three of which are induced by blue light. Nevertheless, structure-function analysis indicates that the biological activity of photl can be attributed to a modular unit comprising the LOV2-kinase region of the protein. Thus, peptide regions upstream of LOV2, including the sites of receptor phosphorylation identified here, do not appear to be important for receptor signaling. By contrast, these regions may be necessary for maximizing stomatal performance and possibly light-induced relocalization of photl.

关键词： Phototropins (phot1 and phot2) lavin-binding motifs

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