Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052278 | FEBS Letters | 2005 | 5 Pages |
Abstract
Phytochromes, photoreceptors controlling important physiological processes in plants and many prokaryotes, are photochromic biliproteins. The red-absorbing Pr ground state is converted by light into the farred-absorbing Pfr which can be photoconverted back to Pr. In plants at least Pfr is the physiologically active signalling state. Here, we show that the N-terminal photochromic module of Cph1 homodimerises reversibly and independently in Pr and Pfr, Pfr-dimers being significantly more stable. Implications for the mechanism of signal transduction are discussed.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Holger M. Strauss, Peter Schmieder, Jon Hughes,