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1 December 2004 Purification and Initial Characterization of a Putative Blue Light–regulated Phosphodiesterase from Escherichia coli
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Abstract

The Escherichia coli protein YcgF contains a photosensory flavin adenine dinucleotide (FAD)–binding BLUF domain covalently linked to an EAL domain, which is predicted to have cyclic-di-guanosine monophosphate (GMP) phosphodiesterase activity. We have cloned, overexpressed and purified this protein, which we refer to as blue light–regulated phosphodiesterase (Blrp) for its putative activity. Blrp undergoes a reversible photocycle after exposure to light in which the spectrum of its photostationary state and kinetics of recovery of the dark state are similar to those of the isolated BLUF domain of the AppA protein. Unlike the AppA BLUF domain, the chromophore environment in the context of full-length Blrp is asymmetric, and the protein does not undergo any detectable global changes on exposure to blue light. When overexpressed in E. coli, Blrp copurifies with certain proteins which suggests that it plays a protective role in response to oxidative stress. Predicted proteins from Klebsiella pneumoniae and from a bacterium in the Sargasso Sea are similar to E. coli Blrp in both their BLUF and EAL domains, which suggests that blue light sensing in these bacteria may follow similar pathways.

Sudarshan Rajagopal, Jason M. Key, Erin B. Purcell, David J. Boerema, and Keith Moffat "Purification and Initial Characterization of a Putative Blue Light–regulated Phosphodiesterase from Escherichia coli," Photochemistry and Photobiology 80(3), 542-547, (1 December 2004). https://doi.org/10.1562/0031-8655(2004)080<0542:PAICOA>2.0.CO;2
Received: 16 June 2004; Accepted: 1 August 2004; Published: 1 December 2004
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