The FMO protein is related to PscA in the reaction center of green sulfur bacteria

被引:6
作者
Olson, JM [1 ]
Raymond, J
机构
[1] Univ Massachusetts, Lederle Grad Res Ctr, Dept Biochem & Mol Biol, Amherst, MA 01003 USA
[2] Arizona State Univ, Dept Chem & Biochem, Tempe, AZ 85287 USA
基金
美国国家航空航天局;
关键词
FMO protein; green sulfur bacteria; PscA; reaction center;
D O I
10.1023/A:1023998000396
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The Fenna-Matthews-Olson protein is a water-soluble protein found only in green sulfur bacteria. Each subunit contains seven bacteriochlorophyll ( BChl) a molecules wrapped in a string bag of protein consisting of mostly beta sheet. Most other chlorophyll-binding proteins are water-insoluble proteins containing membrane-spanning a helices. We compared an FMO consensus sequence to well-characterized, membrane-bound chlorophyll-binding proteins: L & M (reaction center proteins of proteobacteria), D1 & D2 ( reaction center proteins of PS II), CP43 & CP47 (core proteins of PS II), PsaA & PsaB ( reaction center proteins of PS I), PscA (reaction center protein of green sulfur bacteria), and PshA (reaction center protein of heliobacteria). We aligned the FMO sequence with the other sequences using the PAM250 matrix modified for His binding-site identities and found a signature sequence (LxHHxxxGxFxxF) common to FMO and PscA. (The two His residues are BChl a. binding sites in FMO.) This signature sequence is part of a 220-residue C-terminal segment with an identity score of 13%. PRSS (Probability of Random Shuffle) analysis showed that the 220-residue alignment is better than 96% of randomized alignments. This evidence supports the hypothesis that FMO protein is related to PscA.
引用
收藏
页码:277 / 285
页数:9
相关论文
共 24 条
[1]   PHOTOSYNTHETIC REACTION CENTER GENES IN GREEN SULFUR BACTERIA AND IN PHOTOSYSTEM-1 ARE RELATED [J].
BUTTNER, M ;
XIE, DL ;
NELSON, H ;
PINTHER, W ;
HAUSKA, G ;
NELSON, N .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (17) :8135-8139
[2]   NUCLEOTIDE-SEQUENCE OF PSBC, THE GENE ENCODING THE CP-43 CHLOROPHYLL A-BINDING PROTEIN OF PHOTOSYSTEM-II, IN THE CYANOBACTERIUM SYNECHOCYSTIS-6803 [J].
CHISHOLM, D ;
WILLIAMS, JGK .
PLANT MOLECULAR BIOLOGY, 1988, 10 (04) :293-301
[3]  
DAURATLARROQUE ST, 1986, J BIOL CHEM, V261, P3607
[4]  
Dayhoff M.O., 1978, ATLAS PROTEIN SEQ ST, V5
[5]  
DRACHEVA S, 1992, RES PHOTOSYNTHESIS, V1, P53
[6]   The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium [J].
Eisen, JA ;
Nelson, KE ;
Paulsen, IT ;
Heidelberg, JF ;
Wu, M ;
Dodson, RJ ;
Deboy, R ;
Gwinn, ML ;
Nelson, WC ;
Haft, DH ;
Hickey, EK ;
Peterson, JD ;
Durkin, AS ;
Kolonay, JL ;
Yang, F ;
Holt, I ;
Umayam, LA ;
Mason, T ;
Brenner, M ;
Shea, TP ;
Parksey, D ;
Nierman, WC ;
Feldblyum, TV ;
Hansen, CL ;
Craven, MB ;
Radune, D ;
Vamathevan, J ;
Khouri, H ;
White, O ;
Gruber, TM ;
Ketchum, KA ;
Venter, JC ;
Tettelin, H ;
Bryant, DA ;
Fraser, CM .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (14) :9509-9514
[7]   Amyloid fibrils from muscle myoglobin -: Even an ordinary globular protein can assume a rogue guise if conditions are right. [J].
Fändrich, M ;
Fletcher, MA ;
Dobson, CM .
NATURE, 2001, 410 (6825) :165-166
[8]   BNaC1 and BNaC2 constitute at new family of human neuronal sodium channels related to degenerins and epithelial sodium channels [J].
GarciaAnoveros, J ;
Derfler, B ;
NevilleGolden, J ;
Hyman, BT ;
Corey, DP .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (04) :1459-1464
[9]   ANALYSIS OF AMINO-ACID SUBSTITUTION DURING DIVERGENT EVOLUTION - THE 400 BY 400 DIPEPTIDE SUBSTITUTION MATRIX [J].
GONNET, GH ;
COHEN, MA ;
BENNER, SA .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1994, 199 (02) :489-496
[10]   STABLE PHOTOBLEACHING OF P840 IN CHLOROBIUM REACTION-CENTER PREPARATIONS - PRESENCE OF THE 42-KDA BACTERIOCHLOROPHYLL ALPHA-PROTEIN AND A 17-KDA POLYPEPTIDE [J].
HAGERBRAUN, C ;
XIE, DL ;
JAROSCH, U ;
HEROLD, E ;
BUTTNER, M ;
ZIMMERMANN, R ;
DEUTZMANN, R ;
HAUSKA, G ;
NELSON, N .
BIOCHEMISTRY, 1995, 34 (29) :9617-9624