NDLI: Photocycle features of heterologously expressed and assembled eukaryotic flavin-binding BLUF domains of photoactivated adenylyl cyclase (PAC), a blue-light receptor in Euglena gracilis

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Photochemical & Photobiological Sciences Vol - 4 Issue - 8

Photochemical & Photobiological Sciences Vol - 4 Issue - 7

Photochemical & Photobiological Sciences Vol - 4 Issue - 6

Photochemical & Photobiological Sciences Vol - 4 Issue - 5

Photochemical & Photobiological Sciences Vol - 4 Issue - 4

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Photochemical & Photobiological Sciences Vol - 4 Issue - 2

Photochemical & Photobiological Sciences Vol -3

Photochemical & Photobiological Sciences Vol -2

Photocycle features of heterologously expressed and assembled eukaryotic flavin-binding BLUF domains of photoactivated adenylyl cyclase (PAC), a blue-light receptor in Euglena gracilis

Content Provider	Royal Society of Chemistry (RSC)
Author	Takahashi, Tetsuo Iseki, Mineo Ito, Shinji Shiga, Kiyoshi Nishina, Yasuzo Higashi, Shoichi Murakami, Akio Sato, Kyosuke Watanabe, Masakatsu
Copyright Year	2005
Abstract	Photoactivated adenylyl cyclase (PAC) is a recently discovered blue-light photoreceptor that mediates photomovement in Euglena gracilis (Iseki et al., Nature, 2002, 415, 1047–1051). PAC appears to be a heterotetramer composed of two FAD-binding subunits (PACα and PACβ). Both subunits have a pair of homologous regions (F1 and F2) which show homology with prokaryotic “sensors of blue-light using FAD” (BLUF) domains. The F1 and F2 domains of PAC are the only eukaryotic BLUF domains found thus far. We obtained soluble recombinant F1 and F2 proteins in PACα by heterologous expression with fused glutathione-S-transferase (GST) in E. coli. The expressed F1 samples did not bind flavins, but the F2 samples contained both FAD and FMN with trace amounts of riboflavin. We also assembled the histidine-tagged recombinant F2 (6His-F2) from inclusion bodies in E. coli with exogenous FAD or FMN. Blue-light-induced changes in absorption spectra of these assembled samples were highly similar to those reported for prokaryotic BLUF domains. The FAD- or FMN-assembled 6His-F2 photocycled with nearly the same rate constants of light-reaction and dark-relaxation, which were slightly lower than those of GST-cleaved F2. The estimated quantum efficiency for the phototransformation was 0.28–0.32, and the half-life was 34–44 s at 25 °C for the recombinant PACα F2, whereas that reported for prokaryotic BLUF domains varied from ca. 3.5 s (Tll0078) to ca. 900 s (AppA). The mutated recombinant Y472F and Q514G of PACα F2 and the F2 domain of the PACα homologue from Eutreptiella gymnastica, which lacks the Gln residue conserved in other BLUF domains, showed no photoinduced transformation.
Starting Page	762
Ending Page	769
Page Count	8
File Format	HTM / HTML PDF
ISSN	1474905X
Volume Number	4
Issue Number	9
Journal	Photochemical & Photobiological Sciences
DOI	10.1039/b505792b
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Subscribed
Subject Keyword	Iseki Heterotetramer Adenylyl cyclase Escherichia coli Eukaryote Riboflavin Eutreptiella gymnastica Flavin group Sequence homology Euglena Gracilis muscle Flavin mononucleotide PAC Inclusion bodies Quantum mechanics Prokaryote Half-life Flavin adenine dinucleotide Glutathione S-transferase Photoreceptor protein Glutamine
Content Type	Text
Resource Type	Article
Subject	Physical and Theoretical Chemistry

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Photoactivated adenylyl cyclase (PAC) genes in the flagellate Euglena gracilis mutant strains

Heterologous Expression of Photoactivated Adenylyl Cyclase (PAC) Genes from the Flagellate Euglena gracilis in Insect Cells

The origin of photoactivated adenylyl cyclase (PAC), the Euglena blue-light receptor: phylogenetic analysis of orthologues of PAC subunits from several euglenoids and trypanosome-type adenylyl cyclases from Euglena gracilis

Differentiation of photocycle characteristics of flavin -binding BLUF domains of α- and β-subunits of photoactivated adenylyl cyclase of Euglena gracilis

Effects of riboflavin deficiency upon concentrations of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in Novikoff hepatoma in rats.

Riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in human plasma and erythrocytes at baseline and after low-dose riboflavin supplementation.

Regulation of riboflavin-metabolizing enzymes in riboflavin deficiency.

Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in human plasma by capillary electrophoresis and laser-induced fluorescence detection.

Mechanistic insights in light-induced cAMP production by photoactivated adenylyl cyclase alpha (PACalpha).

Photocycle features of heterologously expressed and assembled eukaryotic flavin-binding BLUF domains of photoactivated adenylyl cyclase (PAC), a blue-light receptor in Euglena gracilis

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