The complete amino acid sequence of the antenna polypeptide B806‐866‐β from the cytoplasmic membrane of the green bacterium Chloroflexus auranliacus

FEBS Letters

Zuber, H.¹  Wechsler, T.D.¹  Frank, G.¹  Suter, F.¹  Brunisholz, R.A.¹ 

[1] Institut für Molekularbiologie und Biophysik, ETH-Hönggerberg, CH-8093 Zürich, Switzerland

关键词: Green photosynthetic bacterium;    B806–866 antenna complex;    Light-harvesting polypeptide;    Amino acid sequence;    (Chloroflexus aurantiacus);    BChl;    bacteriochlorophyll;    PTH;    phenylthiohydantoin;    C/M/NH4OAc;    1:1 (v/v) chloroform/methanol containing 0.1 M ammonium acetate;    TFA;    trifluoroacetic acid;    Hfo;    formic acid;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(87)81335-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The bacteriochlorophyll a-binding polypeptide B806–866-β was extracted from membranes of the green thermophilic bacterium Chloroflexus aurantiacus with chloroform/methanol/ammonium acetate. Purification of the antenna polypeptide (6.3 kDa) was achieved by chromatography on Sephadex LH-60, Whatman DE-32 and by FPLC. The complete amino acid sequence (53 amino acid residues) was determined. The B806–866-β polypeptide is sequence homologous to the antenna β-polypeptides of purple bacteria (27–40%) and exhibits the characteristic three domain structure of the B870, B800–850 and B800–820 antenna complexes. The two typical His residues, conserved in all antenna β-polypeptides of purple bacteria, were found: His-24 lies within the N-terminal hydrophilic domain and His-42 within the central hydrophobic domain. This polypeptide together with the previously described α-polypeptide form the basic structural unit of the B806–866 antenna complex from C. aurantiacus.

【 授权许可】

Unknown