Structural and spectroscopic properties of a reaction center complex from the chlorosome-lacking filamentous anoxygenic phototrophic bacterium Roseiflexus castenholzii.
The photochemical reaction center (RC) complex of Roseiflexus castenholzii, which belongs to the filamentous anoxygenic phototrophic bacteria (green filamentous bacteria) but lacks chlorosomes, was isolated and characterized. The genes coding for the subunits of the RC and the light-harvesting proteins were also cloned and sequenced. The RC complex was composed of L, M, and cytochrome subunits. The cytochrome subunit showed a molecular mass of approximately 35 kDa, contained hemes c, and functioned as the electron donor to the photo-oxidized special pair of bacteriochlorophylls in the RC. The RC complex appeared to contain three molecules of bacteriochlorophyll and three molecules of bacteriopheophytin, as in the RC preparation from Chloroflexus aurantiacus. Phylogenetic trees based on the deduced amino acid sequences of the RC subunits suggested that R. castenholzii had diverged from C. aurantiacus very early after the divergence of filamentous anoxygenic phototrophic bacteria from purple bacteria. Although R. castenholzii is phylogenetically related to C. aurantiacus, the arrangement of its puf genes, which code for the light-harvesting proteins and the RC subunits, was different from that in C. aurantiacus and similar to that in purple bacteria. The genes are found in the order pufB, -A, -L, -M, and -C, with the pufL and pufM genes forming one continuous open reading frame. Since the photosynthetic apparatus and genes of R. castenholzii have intermediate characteristics between those of purple bacteria and C. aurantiacus, it is likely that they retain many features of the common ancestor of purple bacteria and filamentous anoxygenic phototrophic bacteria.
Yamada
Mitsunori
M
Department of Biology, Tokyo Metropolitan University, Minamiohsawa, Hachioji, Tokyo, Japan. myamada2@buffalo.edu
Zhang
Hui
H
Hanada
Satoshi
S
Nagashima
Kenji V P
KV
Shimada
Keizo
K
Matsuura
Katsumi
K
D000595:Amino Acid Sequence; D001483:Base Sequence; D041862:Chloroflexi / Q000737:chemistry* / Q000235:genetics; D003001:Cloning, Molecular; D019143:Evolution, Molecular; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D010802:Phylogeny; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013056:Spectrophotometry, Ultraviolet
D045322:Photosynthetic Reaction Center Complex Proteins
J Bacteriol. 1982 May;150(2):905-15
7068536
Nature. 1970 Aug 15;227(5259):680-5
5432063
Proc Natl Acad Sci U S A. 1983 Jan;80(1):80-4
16593269
Arch Microbiol. 1995 Feb;163(2):124-30
7535995
FEBS Lett. 1988 May 23;232(2):364-8
3288502
Biochimie. 1996;78(5):364-9
8905155
FEBS Lett. 2003 Jan 30;535(1-3):166-70
12560097
J Biochem. 1985 Aug;98(2):465-73
3905785
Ann N Y Acad Sci. 1964 Dec 28;121:404-27
14240539
Syst Appl Microbiol. 1987;9:47-53
11542088
Proc Natl Acad Sci U S A. 1987 Sep;84(17):6162-6
2819866
Photosynth Res. 1992;33:91-111
11538390
Biochemistry. 1990 Jun 26;29(25):5881-9
2200518
Arch Microbiol. 1985 Jul;142(2):164-7
2412519
Eur J Biochem. 1991 Jul 15;199(2):317-23
1649048
J Cell Biochem. 1983;22(4):251-61
6671994
Int J Syst Evol Microbiol. 2002 Jan;52(Pt 1):187-93
11837302
Arch Microbiol. 1974;100(1):5-24
4374148
Nature. 1985 Dec 19-1986 Jan 1;318(6047):618-24
22439175
Hoppe Seylers Z Physiol Chem. 1984 Jul;365(7):689-701
6434397
EMBO J. 1987 Aug;6(8):2197-202
16453786
FEBS Lett. 1988 Apr 11;231(1):237-42
2834225
Plant Cell Physiol. 2001 Dec;42(12):1355-62
11773528
EMBO J. 1986 Jun;5(6):1149-58
15966102
Eur J Biochem. 1989 Mar 1;180(1):75-84
2651125
J Biol Chem. 1992 Apr 5;267(10):6531-40
1313011
FEBS Lett. 1990 Jan 29;260(2):165-8
2404796
Nucleic Acids Res. 1994 Nov 11;22(22):4673-80
7984417
Proc Natl Acad Sci U S A. 1982 Nov;79(21):6532-6
16593246
Anal Biochem. 1976 Sep;75(1):168-76
822747
Biochemistry. 1991 Dec 3;30(48):11451-8
1660302
Eur J Biochem. 1987 Sep 15;167(3):595-600
3308462
Proc Natl Acad Sci U S A. 1987 Aug;84(16):5730-4
3303032