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Plant and Cell Physiology 2004 45(12):1729-1737; doi:10.1093/pcp/pch214
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© 2004 Oxford University Press

Rapid Paper

Cyanobacterial Phytochrome-like PixJ1 Holoprotein Shows Novel Reversible Photoconversion Between Blue- and Green-absorbing Forms

Shizue Yoshihara1, Mitsunori Katayama, Xiaoxing Geng and Masahiko Ikeuchi2

Department of Life Sciences (Biology), University of Tokyo, Komaba 3-8-1, Meguro, Tokyo, 153-8902 Japan

The gene, pixJ1 (formerly pisJ1), is predicted to encode a phytochrome-like photoreceptor that is essential for positive phototaxis in the unicellular cyanobacterium Synechocystis sp. PCC 6803 [Yoshihara et al. (2000) Plant Cell Physiol. 41: 1299]. The PixJ1 protein was overexpressed as a fusion with a poly-histidine tag (His–PixJ1) and isolated from Synechocystis cells. A zinc-fluorescence assay suggested that a linear tetrapyrrole was covalently attached to the His–PixJ1 protein as a chromophore. His–PixJ1 showed novel photoreversible conversion between a blue light-absorbing form (Pb, {lambda}Amax = 425–435 nm) and a green light-absorbing form (Pg, {lambda}Amax = 535 nm). Dark incubation led Pg to revert to Pb, indicative of stability of the Pb form in darkness. Red or far-red light irradiation, which is effective for photochemical conversion of the known phytochromes, produced no change in the spectra of Pb and Pg forms. Site-directed mutagenesis revealed that a Cys-His motif in the second GAF domain of PixJ1 is responsible for binding of the chromophore. Possible chromophore species are discussed with regard to the novel photoconversion spectrum.

1 Present address: Research Institute for Advanced Science and Technology, Osaka Prefecture University, 1-2 Gakuen-cho, Sakai, Osaka, 599-8570 Japan.

2 Corresponding author: E-mail, mikeuchi{at}bio.c.u-tokyo.ac.jp; Fax, +81-3-5454-4337.


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