Project description:Viscum album is known for its special mode of cellular respiration. It lacks the mitochondrial NADH dehydrogenase complex (complex I of the respiratory chain) and has restricted capacities to generate mitochondrial adenosine triphosphate (ATP). We here present an investigation of the V. album energy metabolism taking place in mitochondria. Mitochondria were purified from young V. album leaves and membrane bound protein complexes characterized by Blue native polyacrylamide gel electrophoresis as well as by the complexome profiling approach. Proteins were systematically identified by label-free quantitative shotgun proteomics.
Project description:Viscum album is known for its special mode of cellular respiration. It lacks the mitochondrial NADH dehydrogenase complex (complex I of the respiratory chain) and has restricted capacities to generate mitochondrial adenosine triphosphate (ATP). We here present an investigation of the V. album energy metabolism taking place in the chloroplasts. Thylakoids were purified from young V. album leaves and membrane bound protein complexes characterized by Blue native polyacrylamide gel electrophoresis as well as by the complexome profiling approach. Proteins were systematically identified by label-free quantitative shotgun proteomics.
Project description:Outer Membrane Vesicles (OMVs) are spherical bodies derived from the outer membrane of Gram-negative bacteria. Fully encapsulated by membrane, these extracellular structures transport cargo, often proteins, from within the bacterium into the external environment. Although there are multiple studies of OMVs released by pathogenic bacteria, the biogenesis and physiological role of OMVs released by environmental microorganisms is less understood. From a TEM screening of 8 methanotrophs affiliated with both Alpha- and Gammaproteobacteria, OMVs were only detected around cells of Methylomicrobium album BG8. OMVs were formed regardless of carbon or nitrogen source, amount of trace metal availability, or growth phase. The size and morphology of M. album BG8 OMVs were similar well-characterized OMVs from other Gram-negative bacteria. The OMVs were isolated from M. album BG8 cultures and their associated proteome revealed an abundance of membrane-associated proteins, transporters related to calcium uptake, and proteins related to Type I secretion systems (T1SS), such as TolC and RTX, suggesting mediation of cargo selection by the T1SS. This information provides clues to the biogenesis pathway and physiological function of OMVs in M. album BG8.
