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Chromophore-bearing NH_2-terminal domains of phytochromes A and B determine their photosensory specificity and differential light lability

Wagner, Doris and Fairchild, Craig D. and Kuhn, Robert M. and Quail, Peter H. (1996) Chromophore-bearing NH_2-terminal domains of phytochromes A and B determine their photosensory specificity and differential light lability. Proceedings of the National Academy of Sciences of the United States of America, 93 (9). pp. 4011-4015. ISSN 0027-8424. https://resolver.caltech.edu/CaltechAUTHORS:20141203-134442711

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Abstract

In early seedling development, far-red-light-induced deetiolation is mediated primarily by phytochrome A (phyA), whereas red-light-induced deetiolation is mediated primarily by phytochrome B (phyB). To map the molecular determinants responsible for this photosensory specificity, we tested the activities of two reciprocal phyA/phyB chimeras in diagnostic light regimes using overexpression in transgenic Arabidopsis. Although previous data have shown that the NH_2-terminal halves of phyA and phyB each separately lack normal activity, fusion of the NH_2-terminal half of phyA to the COOH-terminal half of phyB (phyAB) and the reciprocal fusion (phyBA) resulted in biologically active phytochromes. The behavior of these two chimeras in red and far-red light indicates: (i) that the NH2-terminal halves of phyA and phyB determine their respective photosensory specificities; (ii) that the COOH-terminal halves of the two photoreceptors are necessary for regulatory activity but are reciprocally inter-changeable and thus carry functionally equivalent determinants; and (iii) that the NH_2-terminal halves of phyA and phyB carry determinants that direct the differential light lability of the two molecules. The present findings suggest that the contrasting photosensory information gathered by phyA and phyB through their NH_2-terminal halves may be transduced to downstream signaling components through a common biochemical mechanism involving the regulatory activity of the COOH-terminal domains of the photoreceptors.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1073/pnas.93.9.4011DOIArticle
http://www.pnas.org/content/93/9/4011PublisherArticle
Additional Information:© 1996 National Academy of Sciences. Communicated by Winslow R. Briggs, Carnegie Institution of Washington, Stanford, CA, December 27, 1995 (received for review August 10, 1995). We thank John Wagner and David Dailey for critical reading of the manuscript and valuable suggestions, Yong Xu for useful discussion, Jim Tepperman for help with the antibody production, and David Hantz and the greenhouse staff for expert care of our plants. This research was supported by grants from the Cancer Research Fund of the Damon Runyon-Walter Winchell Foundation (Fellowship DRG-1302 to C.F.) and by Department of Energy Grant FG03-92ER13742, National Institutes of Health Grant GM47475, and U.S. Department of Agriculture Agricultural Research Service Current Research Information Service Grant 5335-21000-006-00D (to P.H.Q.). The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Funders:
Funding AgencyGrant Number
Damon Runyon-Walter Winchell Foundation Cancer Research FundDRG-1302
Department of Energy (DOE)FG03-92ER13742
NIHGM47475
Department of Agriculture5335-21000-006-00D
Subject Keywords:photomorphogenesis; regulatory photoreceptor; structure-function analysis; functional domains; specific degradation
Issue or Number:9
Record Number:CaltechAUTHORS:20141203-134442711
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20141203-134442711
Official Citation:Wagner, D., Fairchild, C. D., Kuhn, R. M., & Quail, P. H. (1996). Chromophore-bearing NH2-terminal domains of phytochromes A and B determine their photosensory specificity and differential light lability. Proceedings of the National Academy of Sciences, 93(9), 4011-4015.
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:52343
Collection:CaltechAUTHORS
Deposited By: Jason Perez
Deposited On:04 Dec 2014 17:44
Last Modified:03 Oct 2019 07:41

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