| Literature DB >> 16922605 |
Rei Narikawa1, Kazunori Zikihara, Koji Okajima, Yuriko Ochiai, Mitsunori Katayama, Yoshinori Shichida, Satoru Tokutomi, Masahiko Ikeuchi.
Abstract
Light, oxygen or voltage (LOV) domains function as blue-light sensors in the phototropin family of photoreceptors found in plants, algae and bacteria. We detected putative LOV domains (Alr3170-LOV, All2875-LOV and Alr1229-LOV) in the genome of a filamentous cyanobacterium, Anabaena sp. PCC 7120. These cyanobacterial LOV domains are closely clustered with the known LOV domains. Alr3170-LOV and A112875-LOV carry the conserved cysteine residue unique to the photoactive LOV, whereas Alr1229-LOV does not. We expressed these three LOV domains in Escherichia coli and purified them. In fact, Alr3170-LOV and A112875-LOV that are conserved in Nostoc punctiforme, a related species, bound flavin mononucleotide and showed spectral changes unique to known LOV domains on illumination with blue light. Alr3170-LOV was completely photoreduced and dark reversion was slow, whereas A112875-LOV was slowly photoreduced and dark reversion was rapid. For comparison, AvA112875-LOV in a closely related A. variabilis was also studied as a homolog of A112875-LOV. Finally, we observed that Alr1229-LOV that is not conserved in N. punctiforme showed no flavin binding.Entities:
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Year: 2006 PMID: 16922605 DOI: 10.1562/2006-05-02-RA-888
Source DB: PubMed Journal: Photochem Photobiol ISSN: 0031-8655 Impact factor: 3.421