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Light-dependent dimerisation in the N-terminal sensory module of cyanobacterial phytochrome 1.
- Source :
-
FEBS letters [FEBS Lett] 2005 Jul 18; Vol. 579 (18), pp. 3970-4. - Publication Year :
- 2005
-
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.
- Subjects :
- Area Under Curve
Biophysical Phenomena
Biophysics
Chromatography
Chromatography, Gel
Dimerization
Dose-Response Relationship, Drug
Internet
Kinetics
Light
Macromolecular Substances chemistry
Photochemistry
Photoreceptor Cells metabolism
Protein Structure, Quaternary
Protein Structure, Tertiary
Scattering, Radiation
Signal Transduction
Ultracentrifugation
Cyanobacteria metabolism
Phytochrome chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 579
- Issue :
- 18
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 16004995
- Full Text :
- https://doi.org/10.1016/j.febslet.2005.06.025