Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1996 Apr 30;93(9):4011-5.
doi: 10.1073/pnas.93.9.4011.

Chromophore-bearing NH2-terminal domains of phytochromes A and B determine their photosensory specificity and differential light lability

Affiliations

Chromophore-bearing NH2-terminal domains of phytochromes A and B determine their photosensory specificity and differential light lability

D Wagner et al. Proc Natl Acad Sci U S A. .

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 NH2-terminal halves of phyA and phyB each separately lack normal activity, fusion of the NH2-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 NH2-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 NH2-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.

PubMed Disclaimer

References

    1. Plant J. 1995 Mar;7(3):413-27 - PubMed
    1. Plant Mol Biol. 1994 Jun;25(3):413-27 - PubMed
    1. Plant Cell. 1993 Jul;5(7):757-68 - PubMed
    1. Plant Cell. 1991 Dec;3(12):1275-1288 - PubMed
    1. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8596-600 - PubMed

Publication types

LinkOut - more resources