Print Email Facebook Twitter Immunogold localization of key metabolic enzymes in the anammoxosome and on the tubule-like structures of Kuenenia stuttgartiensis Title Immunogold localization of key metabolic enzymes in the anammoxosome and on the tubule-like structures of Kuenenia stuttgartiensis Author De Almeida, N.M. Neumann, S. Mesman, R.J. Ferousi, C. Keltjens, J.T. Jetten, M.S.M. Kartal, B. Van Niftrik, L. Faculty Applied Sciences Department BT/Biotechnology Date 2015-12-31 Abstract Anaerobic ammonium-oxidizing (anammox) bacteria oxidize ammonium with nitrite as the terminal electron acceptor to form dinitrogen gas in the absence of oxygen. Anammox bacteria have a compartmentalized cell plan with a central membrane-bound “prokaryotic organelle” called the anammoxosome. The anammoxosome occupies most of the cell volume, has a curved membrane, and contains conspicuous tubule-like structures of unknown identity and function. It was suggested previously that the catalytic reactions of the anammox pathway occur in the anammoxosome, and that proton motive force was established across its membrane. Here, we used antibodies raised against five key enzymes of the anammox catabolism to determine their cellular location. The antibodies were raised against purified native hydroxylamine oxidoreductase-like protein kustc0458 with its redox partner kustc0457, hydrazine dehydrogenase (HDH; kustc0694), hydroxylamine oxidase (HOX; kustc1061), nitrite oxidoreductase (NXR; kustd1700/03/04), and hydrazine synthase (HZS; kuste2859-61) of the anammox bacterium Kuenenia stuttgartiensis. We determined that all five protein complexes were exclusively located inside the anammoxosome matrix. Four of the protein complexes did not appear to form higher-order protein organizations. However, the present data indicated for the first time that NXR is part of the tubule-like structures, which may stretch the whole length of the anammoxosome. These findings support the anammoxosome as the locus of catabolic reactions of the anammox pathway. To reference this document use: http://resolver.tudelft.nl/uuid:d5262251-c27b-4512-a4a7-7309c6ad1a2b DOI https://doi.org/10.1128/JB.00186-15 Publisher American Society for Microbiology ISSN 0021-9193 Source Journal of Bacteriology, 197(14)2015 Part of collection Institutional Repository Document type journal article Rights (c) 2015 The Authors and ASM Files PDF 322956.pdf 6.97 MB Close viewer /islandora/object/uuid:d5262251-c27b-4512-a4a7-7309c6ad1a2b/datastream/OBJ/view