The primary structure of the antenna polypeptides of Ectothiorhodospira halochloris and Ectothiorhodospira halophila. Four core-type antenna polypeptides in E. halochloris and E. halophila.
Antenna polypeptides from two species of the family Ectothiorhodospiraceae have been investigated. By means of gel filtration and subsequent high-performance liquid chromatography, at least five polypeptides were isolated from each of Ectothiorhodospira halochloris and Ectothiorhodospira halophila. The majority of their primary structures was identified by Edman degradation. Comparison of these polypeptide sequences with the known primary structures of antenna polypeptides from various purple non-sulfur bacteria revealed interesting new aspects with regard to the structure of the core-peripheral antenna system. E. halochloris and E. halophila contain two pairs of alpha- and beta-polypeptides each with typical primary structure elements of core complexes, indicating a modified antenna complex organization.
Wagner-Huber
R
R
Institut für Molekularbiologie und Biophysik, ETH-Hönggerberg, Zürich, Switzerland.
Brunisholz
R A
RA
Bissig
I
I
Frank
G
G
Suter
F
F
Zuber
H
H
D000478:Alkylation; D000595:Amino Acid Sequence; D001419:Bacteria / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics*; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003488:Cyanogen Bromide; D045342:Light-Harvesting Protein Complexes; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010455:Peptides / Q000235:genetics* / Q000378:metabolism; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid; D013057:Spectrum Analysis
D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes; D010455:Peptides; D045322:Photosynthetic Reaction Center Complex Proteins; D003488:Cyanogen Bromide