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<b>Abstract</b>— <p>In the RC-LH1 complex of <i>Rhodopseudomonas</i> (<i>Rps.</i>) <i>palustris</i> KM 286 (le5), a γ-protein, which was recently identified in the light-harvesting LH2 complex of this bacterium, was identified by proteomic analysis. For the first time, the method of adsorptive chromatography on hydroxyapatite was developed and&#xa0;applied to isolate RC-LH1. The bioinformatics analysis of <i>Rps. palustris</i> CGA009 (ATCC BAA-98) genome revealed a close location of the genes encoding α-, β-, and γ-proteins and similar functional groups in the γ-proteins of both complexes interacting with bacteriochlorophyll and the α- and β-proteins, which may indicate that γ-proteins have similar functions. The differences in the structure of the LH2 and LH1 complexes leave open the question of the localization of the γ-protein in RC-LH1, which requires further structural studies of this complex.</p>

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A New Protein of the RC-LH1 Complex from the Phototrophic Purple Non-Sulfur Bacterium Rhodopseudomonas palustris

  • 期刊论文

  • 发表日期：

    2026年7月17日

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  • O. P. Serdyuk,
  • E. P. Petushkova,
  • M. Kh. Khasimov

摘要

Abstract—

In the RC-LH1 complex of Rhodopseudomonas (Rps.) palustris KM 286 (le5), a γ-protein, which was recently identified in the light-harvesting LH2 complex of this bacterium, was identified by proteomic analysis. For the first time, the method of adsorptive chromatography on hydroxyapatite was developed and applied to isolate RC-LH1. The bioinformatics analysis of Rps. palustris CGA009 (ATCC BAA-98) genome revealed a close location of the genes encoding α-, β-, and γ-proteins and similar functional groups in the γ-proteins of both complexes interacting with bacteriochlorophyll and the α- and β-proteins, which may indicate that γ-proteins have similar functions. The differences in the structure of the LH2 and LH1 complexes leave open the question of the localization of the γ-protein in RC-LH1, which requires further structural studies of this complex.