FMN binding and photochemical properties of plant putative photoreceptors containing two LOV domains, LOV/LOV proteins.
LOV domains function as blue light-sensing modules in various photoreceptors in plants, fungi, algae, and bacteria. A LOV/LOV protein (LLP) has been found from Arabidopsis thaliana (AtLLP) as a two LOV domain-containing protein. However, its function remains unknown. We isolated cDNA clones coding for an LLP homolog from tomato (Solanum lycopersicum) and two homologs from the moss Physcomitrella patens. The tomato LLP (SlLLP) contains two LOV domains (LOV1 and LOV2 domains), as in AtLLP. Most of the amino acids required for association with chromophore are conserved in both LOV domains, except that the amino acid at the position equivalent to the cysteine essential for cysteinyl adduct formation is glycine in the LOV1 domain as in AtLLP. When expressed in Escherichia coli, SlLLP binds FMN and undergoes a self-contained photocycle upon irradiation of blue light. Analyses using mutant SlLLPs revealed that SlLLP binds FMN in both LOV domains, although the LOV1 domain does not show spectral changes on irradiation. However, when Gly(66) in the LOV1 domain, which is located at the position equivalent to the essential cysteine of LOV domains, is replaced by cysteine, the mutated LOV1 domain shows light-induced spectral changes. In addition, all four LOV domains of P. patens LLPs (PpLLP1 and PpLLP2) show the typical features of LOV domains, including the reactive cysteine in each. This study shows that plants have a new LOV domain-containing protein family with the typical biochemical and photochemical properties of other LOV domain-containing proteins such as the phototropins.
Kasahara
Masahiro
M
Department of Biotechnology, College of Life Sciences, Ritsumeikan University, Nojihigashi, Kusatsu, Shiga 525-8577, Japan. kasa@sk.ritsumei.ac.jp
Torii
Mayumi
M
Fujita
Akimitsu
A
Tainaka
Kengo
K
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism; D019068:Bryopsida / Q000235:genetics / Q000378:metabolism*; D005486:Flavin Mononucleotide / Q000235:genetics / Q000378:metabolism*; D008027:Light; D018551:Solanum lycopersicum; D008969:Molecular Sequence Data; D056949:Phototropins / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism
D056949:Phototropins; D011994:Recombinant Proteins; D005486:Flavin Mononucleotide
J Plant Res. 2008 Jan;121(1):97-105
17982713
Annu Rev Plant Biol. 2007;58:21-45
17067285
Nucleic Acids Res. 2010 Jan;38(Database issue):D211-22
19920124
Proc Natl Acad Sci U S A. 2007 Dec 4;104(49):19625-30
18003911
Proc Natl Acad Sci U S A. 1999 Jul 20;96(15):8779-83
10411952
Biochim Biophys Acta. 2008 Jan;1784(1):133-42
17988963
J Biomed Sci. 2007 Jul;14(4):499-504
17380429
Plant Physiol. 2002 Jun;129(2):762-73
12068117
Biopolymers. 2006 Jul;82(4):373-8
16552739
Biochemistry. 2007 Mar 20;46(11):3129-37
17311415
Plant Signal Behav. 2008 Nov;3(11):966-8
19704421
Nature. 2003 Nov 20;426(6964):302-6
14628054
Plant Cell. 2001 Dec;13(12):2659-70
11752379
Biochemistry. 2003 Jan 14;42(1):2-10
12515534
FEBS Lett. 2009 Feb 4;583(3):526-30
19166850
Science. 2007 Aug 24;317(5841):1090-3
17717187
Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13337-42
16150710
Nucleic Acids Res. 1988 Aug 11;16(15):7351-67
3045756
Photochem Photobiol. 2006 Nov-Dec;82(6):1627-33
16922605
EMBO J. 2003 Sep 15;22(18):4846-55
12970196
Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):2995-3000
11248020
Cell. 2000 Apr 28;101(3):331-40
10847687
Planta. 2009 Aug;230(3):543-52
19544070
Biochemistry. 2000 Aug 8;39(31):9401-10
10924135
Proc Natl Acad Sci U S A. 2001 Jun 5;98(12):6969-74
11371609
Cell. 2000 Apr 28;101(3):319-29
10847686
Proc Natl Acad Sci U S A. 2007 Nov 13;104(46):18241-6
17986614
Biophys J. 2003 Apr;84(4):2474-82
12668455