Journal article

Publication year: 2005

Pages: 3970-3974

Journal: FEBS Letters

Volume number: 579

Issue number: 18

ISSN: 1873-3468

DOI Link: https://doi.org/10.1016/j.febslet.2005.06.025

Publisher: Wiley

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. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

Harvard Citation style: Strauss, H., Schmieder, P. and Hughes, J. (2005) Light-dependent dimerisation in the N-terminal sensory module of cyanobacterial phytochrome 1, FEBS Letters, 579(18), pp. 3970-3974. https://doi.org/10.1016/j.febslet.2005.06.025

APA Citation style: Strauss, H., Schmieder, P., & Hughes, J. (2005). Light-dependent dimerisation in the N-terminal sensory module of cyanobacterial phytochrome 1. FEBS Letters. 579(18), 3970-3974. https://doi.org/10.1016/j.febslet.2005.06.025