Abstract:
:Plants employ a variety of light, oxygen, voltage (LOV) domain photoreceptors to regulate diverse aspects of growth and development. The Zeitlupe (ZTL), Flavin-Kelch-Fbox-1 (FKF1), and LOV-Kelch-Protein-2 (LKP2) proteins dictate measurement of the day length, flowering time, and regulation of the circadian clock by blue-light regulation of protein complex formation. Previous reports indicated that ZTL photochemistry was irreversible, which is inconsistent with its role in marking the day-night transition. A kinetic model of LOV domain function predicts that ZTL has evolved unique photochemical parameters to allow it to function as a sensor of environmental light intensity. Moreover, our model indicates that a photocatalyzed reverse reaction is required for the sensitivity of LOV domains to light fluence. Inclusion of a photocatalyzed rate constant allows the establishment of a photostationary steady state of light-activated proteins, whose relative population is sensitive to daily (circadian) or positional (phototropism) oscillations in light intensity. Photochemical characterization confirms that ZTL undergoes adduct decay on a time scale of hours in contrast to previous reports. The fast photocycle allows detection of the day-night transition facilitating circadian timing. ZTL kinetics reflect an evolutionary adaptation of the ZTL/FKF1/LKP2 family to function in distinct aspects of blue-light signaling.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Pudasaini A,Zoltowski BDdoi
10.1021/bi401027nsubject
Has Abstractpub_date
2013-10-08 00:00:00pages
7150-8issue
40eissn
0006-2960issn
1520-4995journal_volume
52pub_type
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