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PMID: 19109976 Published · ppublish English Journal Article Research Support, N.I.H., Extramural

Design and signaling mechanism of light-regulated histidine kinases.

Journal of molecular biology ·Vol. 385 ·No. 5 ·2009-02-06 ·Pages 1433-44

Möglich A, Ayers RA, Moffat K

Abstract

Signal transduction proteins are organized into sensor (input) domains that perceive a signal and, in response, regulate the biological activity of effector (output) domains. We reprogrammed the input signal specificity of a normally oxygen-sensitive, light-inert histidine kinase by replacing its chemosensor domain by a light-oxygen-voltage photosensor domain. Illumination of the resultant fusion kinase YF1 reduced net kinase activity by approximately 1000-fold in vitro. YF1 also controls gene expression in a light-dependent manner in vivo. Signals are transmitted from the light-oxygen-voltage sensor domain to the histidine kinase domain via a 40 degrees -60 degrees rotational movement within an alpha-helical coiled-coil linker; light is acting as a rotary switch. These signaling principles are broadly applicable to domains linked by alpha-helices and to chemo- and photosensors. Conserved sequence motifs guide the rational design of light-regulated variants of histidine kinases and other proteins.

MeSH Terms
Amino Acid Sequence Escherichia coli/enzymology Histidine Kinase Light Molecular Sequence Data Phosphorylation Protein Kinases/chemistry,genetics,physiology Protein Structure, Secondary Recombinant Fusion Proteins/chemistry,genetics,physiology Signal Transduction
Chemicals
Recombinant Fusion Proteins Protein Kinases Histidine Kinase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Möglich Andreas
Department of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637, USA.
Ayers Rebecca A
Moffat Keith
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Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
1089-8638
Published
2009-02-06
Epub
2008-00-14
Pages
1433-44
Language
English
Region
England
NLM ID
2985088R
PMCID
PMC3527124
Subset
IM
Grants
NIGMS NIH HHS · R01 GM036452 · United States
NIGMS NIH HHS · R37 GM036452 · United States
NIGMS NIH HHS · GM036452 · United States
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