Project description:A biohydrogen and polyhydroxyalkanoates(PHA)-producing natural photoheterotrophic mixed culture composed mainly by Rhodopseudomonas palustris and Clostridium sp was studied by a proteomic analysis under non-growth conditions (nitrogen-absence and organic acids). Proteins in C. pasteurianum were upregulated, particularly those related to stress response. In contrast, C. pasteurianum in the consortium did not present such proteins, showing the advantage of being part of it. Both cultures showed proteins involved in organic acid metabolism and biohydrogen production, such as lactate dehydrogenase, ferredoxins, and hydrogenases. Proteomes of R. palustris as single culture and in consortium showed that organic acids were redirect into central carbon pathways to generate reduced equivalents for biohydrogen production. Light-harvesting proteins and fatty acid metabolism linked to PHA accumulation were also upregulated. This study provides insights into how the proteomes of individual organisms and their consortium counterparts adapt to non-growth conditions, shedding light on how microbial interactions influence protein expression.
Project description:The purple bacterium Rhodopseudomonas palustris is a model organism for dissecting the energy and electron transfer processes that have evolved in phototrophic organisms. This bacterium is of particular interest because, in addition to driving its metabolism via solar energy capture, it is capable of nitrogen and carbon dioxide fixation, producing hydrogen and utilising a wide range of organic compounds. Understanding these processes underpins the potential exploitation of Rhodopseudomonas palustris for synthetic biology, biohydrogen production and bioremediation, for example. Like other purple bacteria, Rhodopseudomonas palustris has 2 light-harvesting (LH) systems: LH1 and LH2. The former has already been extensively characterised by X-ray crystallography and cryo-EM. The aim of this proteomics project is to provide complementary information to support the cryo-EM mapping of LH2 structure.