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

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.

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Journal
Microbiology
Published
2026-07-17
DOI
https://doi.org/10.1134/s0026261725605627
Primary Topic
Photosynthetic Processes and Mechanisms
Type
article
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article

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

O. P. Serdyuk, Е. П. Петушкова, М. Х. Хасимов
Microbiology
Photosynthetic Processes and Mechanisms
article

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

O. P. Serdyuk, Е. П. Петушкова, М. Х. Хасимов
article en

Abstract

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.

MicrobiologyVol. 95(4)
Institute of Basic Biological Problems (RU)
Openalex Percentile: Top 14%
Photosynthetic Processes and Mechanisms
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