Light Modulation of Cellular cAMP by a Small Bacterial Photoactivated Adenylyl Cyclase, bPAC, of the Soil Bacterium Beggiatoa

The recent success of channelrhodopsin in optogenetics has also caused increasing interest in enzymes that are directly activated by light. We have identified in the genome of the bacterium Beggiatoa a DNA sequence encoding an adenylyl cyclase directly linked to a BLUF (blue light receptor using FAD...

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Bibliographic Details
Published in:The Journal of biological chemistry 2011-01, Vol.286 (2), p.1181-1188
Main Authors: Stierl, Manuela, Stumpf, Patrick, Udwari, Daniel, Gueta, Ronnie, Hagedorn, Rolf, Losi, Aba, Gärtner, Wolfgang, Petereit, Linda, Efetova, Marina, Schwarzel, Martin, Oertner, Thomas G., Nagel, Georg, Hegemann, Peter
Format: Article
Language:English
Subjects:
Adenylyl Cyclases - genetics
Adenylyl Cyclases - metabolism
Adenylyl Cyclases - radiation effects
Amino Acid Sequence
Animals
Animals, Genetically Modified
Bacterial Metabolism
Beggiatoa
Beggiatoa - enzymology
Beggiatoa - genetics
Biophysics
Cyclic AMP (cAMP)
Cyclic AMP - metabolism
Cyclic Nucleotides
Cystic Fibrosis Transmembrane Conductance Regulator - genetics
Drosophila
Drosophila - enzymology
Drosophila - genetics
Enzyme Activation - radiation effects
Enzyme Catalysis
Enzyme Inactivation
Enzymology
Escherichia coli
Escherichia coli - enzymology
Escherichia coli - genetics
Excitatory Postsynaptic Potentials - physiology
Hippocampus - cytology
Humans
Light
Molecular Sequence Data
Neurobiology
Neurons - cytology
Neurons - physiology
Oocytes - physiology
Optogenetics
Photochemistry
Photoreceptors
Rats
Rats, Wistar
Xenopus
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Summary:The recent success of channelrhodopsin in optogenetics has also caused increasing interest in enzymes that are directly activated by light. We have identified in the genome of the bacterium Beggiatoa a DNA sequence encoding an adenylyl cyclase directly linked to a BLUF (blue light receptor using FAD) type light sensor domain. In Escherichia coli and Xenopus oocytes, this photoactivated adenylyl cyclase (bPAC) showed cyclase activity that is low in darkness but increased 300-fold in the light. This enzymatic activity decays thermally within 20 s in parallel with the red-shifted BLUF photointermediate. bPAC is well expressed in pyramidal neurons and, in combination with cyclic nucleotide gated channels, causes efficient light-induced depolarization. In the Drosophila central nervous system, bPAC mediates light-dependent cAMP increase and behavioral changes in freely moving animals. bPAC seems a perfect optogenetic tool for light modulation of cAMP in neuronal cells and tissues and for studying cAMP-dependent processes in live animals.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M110.185496