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Light‐dependent dimerisation in the N‐terminal sensory module of cyanobacterial phytochrome 1
Author(s) -
Strauss Holger M.,
Schmieder Peter,
Hughes Jon
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.06.025
Subject(s) - phytochrome , photochromism , biophysics , terminal (telecommunication) , chemistry , transduction (biophysics) , signal transduction , photochemistry , red light , biochemistry , biology , botany , telecommunications , computer science
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.