Journalartikel

Jahr der Veröffentlichung: 2005

Seiten: 3970-3974

Zeitschrift: FEBS Letters

Bandnummer: 579

Heftnummer: 18

ISSN: 1873-3468

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

Verlag: 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-Zitierstil: 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-Zitierstil: 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