TY - JOUR
T1 - Bacteriophytochromes
T2 - New tools for understanding phytochrome signal transduction
AU - Vierstra, Richard David
AU - Davis, Seth Jon
N1 - Funding Information:
We thank D. Kehoe, M. Tandeau de Mardac, S.-H. Bhoo and A. Vener for providing information prior to publication. Our work was supported by a grant from the U.S. Department of Energy.
PY - 2000
Y1 - 2000
N2 - The recent discovery of phytochrome-like photoreceptors, collectively called bacteriophytochromes, in a number of bacteria has greatly expanded our understanding of the origins and modes of action of phytochromes in higher plants. These primitive receptors contain an N-terminal domain homologous to the chromophore-binding pocket of phytochromes, and like phytochromes, they bind a variety of bilins to generate photochromic holoproteins. Following the chromophore pocket is a domain similar to two-component histidine kinases, suggesting that these bacterial photoreceptors function in phosphorelay cascades that respond to the light environment. Their organization and distribution support the views that higher-plant phytochromes evolved from a cyanobacterial precursor and that they act as light-regulated kinases. With the ability to exploit bacterial genetics, these bacteriophytochromes now offer simple models to help unravel the biochemical and biophysical events that initiate phytochrome signal transmission.
AB - The recent discovery of phytochrome-like photoreceptors, collectively called bacteriophytochromes, in a number of bacteria has greatly expanded our understanding of the origins and modes of action of phytochromes in higher plants. These primitive receptors contain an N-terminal domain homologous to the chromophore-binding pocket of phytochromes, and like phytochromes, they bind a variety of bilins to generate photochromic holoproteins. Following the chromophore pocket is a domain similar to two-component histidine kinases, suggesting that these bacterial photoreceptors function in phosphorelay cascades that respond to the light environment. Their organization and distribution support the views that higher-plant phytochromes evolved from a cyanobacterial precursor and that they act as light-regulated kinases. With the ability to exploit bacterial genetics, these bacteriophytochromes now offer simple models to help unravel the biochemical and biophysical events that initiate phytochrome signal transmission.
KW - Bacteria
KW - Histidine kinase
KW - Light regulation
KW - Phosphorelay
KW - Phytochrome
UR - https://www.scopus.com/pages/publications/0034494048
U2 - 10.1006/scdb.2000.0206
DO - 10.1006/scdb.2000.0206
M3 - Article
C2 - 11145881
AN - SCOPUS:0034494048
SN - 1084-9521
VL - 11
SP - 511
EP - 521
JO - Seminars in Cell and Developmental Biology
JF - Seminars in Cell and Developmental Biology
IS - 6
ER -