Consequences for the Organization of Reaction Center-Light Harvesting Antenna 1 (LH1) Core Complexes of Rhodobacter sphaeroides Arising from Deletion of Amino Acid Residues from the C Terminus of the LH1 α Polypeptide

Abstract

The light harvesting antenna 1 (LH1) complex of Rhodobacter sphaeroides is intimately associated with the reaction center (RC) as part of the reaction center RC-LH1 core complex. The pufA gene has been modified such that between 5 and 16 amino acid residues were progressively deleted from the C terminus of the LH1 alpha polypeptide. The two largest deletions produced strains which were deficient in LH1. The remaining four deletion mutants exhibited significant reductions in the average level of LH1 per reaction center. Analysis of detergent-solubilized cores on sucrose gradients showed that the mutant strains had a sizeable population of antenna-deficient reaction centers in addition to core complexes with a reduced ratio of LH1:RC. The decrease in the ratio of LH1:RC in core complexes of the mutant strains was accompanied by a progressive blue shift of the absorbance maximum of LH1, which we attribute to the reduced aggregation state of LH1 in the smaller cores. The PufX polypeptide was not required for photosynthetic growth in mutants with reduced core sizes. We conclude that the level of LH1 in the bacterial membrane, and the aggregation state of LH1 in core complexes, are both influenced by the C terminus of the alpha polypeptide, and we discuss possible models for the organization of the core complex in Rb. sphaeroides.