The Primary Structures of the Core Antenna Polypeptides from Rhodopseudomonas marina
Open Access
- 1 June 1989
- journal article
- research article
- Published by Walter de Gruyter GmbH in Zeitschrift für Naturforschung C
- Vol. 44 (5-6) , 407-414
- https://doi.org/10.1515/znc-1989-5-612
Abstract
The antenna complex B 880 of Rp marina has been isolated by applying ion-exchange chromatography on Whatman DE-52 resin and sucrose density centrifugation of LDAO-solubilized photosynthetic membranes. The antenna polypeptides B 880-.alpha. and B 880-.beta. were prepared by organic solvent extraction of extensively dialyzed and freeze-dried B 880 antenna complex material or photosynthetic membranes. Gel filtration on Sephadex LH-60 and ion-exchange chromatography on Whatman DE-32 resin in the presence of organic solvents and an additional step on a C-8 reversed phase column yield pure .alpha.- and .beta.-apoproteins. Their complete primary structures have been elucidated using automated Edman degradation and carboxypeptidase digestion. According to quantitative Edman degradation the ratio of B 880-.alpha. and B 880-.beta. has been determined as 1:1 in the isolated antenna complex as well as in the photosynthetic membrane. B 880-.alpha. of Rp. marina, presumably N-formylated, consists of 52 amino acid residues and is 75.56, 52 and 44% homologous to the corresponding core antenna polypeptides of Rhodospirillum rubrum; Rp. Viridis, Rhodobacter capsulatus and Rb. sphaeroides. In contrast, B 880-.beta. (56 amino acid residues) is less homologous to the corresponding core .beta.-antenna polypeptides of the same strains (57, 51, 41 and 42%). It shows an extended N-terminal domain as compared to the B 880-.alpha. polypeptide. Apart from the typical structural features of bacterial membrane-bound antenna polypeptides (three domain structure, His-residue in the hydrophobic stretch) the antenna polypeptides of Rp. marina are structurally related to polypeptides of core antenna complexes with strong near infrared circular dichroism signals.Keywords
This publication has 6 references indexed in Scilit:
- The Light-Harvesting Polypeptides ofRhodopseudomonas viridis.The Complete Amino-Acid Sequences of B1015-α, B1015-β and B1015-γBiological Chemistry Hoppe-Seyler, 1985
- The Light-Harvesting Polypeptides ofRhodopseudomonas sphaeroidesR-26.1. I. Isolation, Purification and Sequence AnalysesHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1984
- The Light-Harvesting Polypeptides ofRhodospirillum rubrum.II. Localisation of the Amino-Terminal Regions of the Light-Harvesting Polypeptides B 870-α and B 870-β and the Reaction-Centre Subunit L at the Cytoplasmic Side of the Photosynthetic Membrane ofRhodospirillum rubrumG-9+Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1984
- The Light-Harvesting Polypeptides ofRhodospirillum rubrum.I. The Amino-Acid Sequence of the Second Light-Harvesting Polypeptide B 880-β (B 870-β) ofRhodospirillum rubrumS 1 and the Carotenoidless Mutant G-9+. Aspects of the Molecular Structure of the two Light-Harvesting Polypeptides B 880-α (B 870-α) and B 880-β (B 870-β) and of the Antenna Complex B 880 (B 870) fromRhodospirillum rubrumHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1984
- Rhodopseudomonas marina sp. nov., a New Marine Phototrophic Purple BacteriumSystematic and Applied Microbiology, 1983
- The Complete Amino‐Acid Sequence of the Large BacteriochlorophyII‐Binding Polypeptide from Light‐Harvesting Complex II (B800—850) of Rhodopseudomonas capsulataEuropean Journal of Biochemistry, 1983