Abstract
The ability of phytochrome to act as a light-regulated molecular switch must initially result from conformational differences between the red light (R)-absorbing Pr and far-red light (FR)-absorbing Pfr forms of the chromoprotein. As a result, much effort has been directed towards characterizing the structure of purified phytochrome and locating domains that change upon photo-conversion in attempts to understand how phytochrome functions. While many interesting structural domains have been identified to date (Chapter 4.3; Vierstra and Quail 1986; Quail 1991), elucidating the role(s) they play in phytochrome action has been hampered by the lack of an in vitro assay suitable for assessing the biological activity of the chromoprotein.
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Further Reading
Boylan M.T. and Quail P.H. (1989) Oat phytochrome is biologically active in transgenic tomatoes. Plant Cell 1: 765–773.
Cherry J.R., Hondred D., Walker J.M. and Vierstra R.D. (1992) Phytochrome requires the 6-kDa N-terminal domain for full biological activity. Proc. Natl. Acad. Sci. USA 89: 5039–5043.
Keller J.M., Shanklin J., Vierstra R.D. and Hershey H.P. (1989) Expression of a functional monocotyledonous phytochrome in transgenic tobacco. EMBOJ. 8:1005–1012.
Nagatani A., Kay S.A., Deak M., Chua N.-H. and Furuya M. (1991) Rice type I phytochrome regulates hypocotyl elongation in transgenic tobacco seedlings. Proc. Natl. Acad. Sci. USA 88: 5207–5211.
Quail P.H. (1991) Phytochrome: A light-activated molecular switch that regulates plant gene expression. Annu. Rev. Genet. 25: 389–409.
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Cherry, J.R., Vierstra, R.D. (1994). The use of transgenic plants to examine phytochrome structure/function. In: Kendrick, R.E., Kronenberg, G.H.M. (eds) Photomorphogenesis in Plants. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-1884-2_11
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DOI: https://doi.org/10.1007/978-94-011-1884-2_11
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