The Primary Structures of the Core Antenna Polypeptides from Rhodopseudomonas marina

Abstract

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-α and B 880-β 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 yielded pure α-and β-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-α and B 880-β has been determined as 1:1 in the isolated antenna complex as well as in the photosynthetic membrane. B 880-α of Rp. marina, presumably N -form ylated, consists of 52 amino acid residues and is 75, 56, 52 and 44% homologous to the corresponding core antenna polypeptides of Rs. rubrum, Rp. viridis, Rb. capsulatus and Rb. sphaeroides. In contrast, B 880-β (56 amino acid residues) is less homologous to the corresponding core β-antenna polypeptides of the same strains (57. 51. 41 and 42%). It shows an extended N-terminal domain as compared to the B 880-a 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.