Cells organize and regulate their metabolism via membrane- or protein-bound organelles. In this way, incompatible processes can be spatially separated and controlled. In prokaryotes, protein-based compartments are used to sequester harmful reactions and store useful compounds. These protein compartments play key roles in various metabolic and ecological processes, ranging from iron homeostasis to carbon fixation. One of the newest types of protein organelle are encapsulin nanocompartments. They are able to encapsulate specific protein cargo and are proposed to be involved in redox-related processes. We identified more than 900 putative encapsulin systems in bacterial and archaeal genomes. Encapsulins can be found in fifteen bacterial and two archaeal phyla. Our analysis reveals one new capsid type and nine previously unknown cargo proteins targeted to the interior of encapsulins. We experimentally characterize three newly identified encapsulin systems and illustrate their probable involvement in iron mineralization, oxidative and nitrosative stress resistance and anaerobic ammonium oxidation, a process responsible for 30% of the nitrogen lost from the oceans.
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This work was supported by a Leopoldina Research Fellowship (LPDS 2014-05) from the German National Academy of Sciences Leopoldina (T.W.G), the DARPA Living Foundries 1000 Molecules grant (award no. HR0011-14-C-0072, to P.A.S) and the Wyss Institute for Biologically Inspired Engineering at Harvard University (to T.W.G and P.A.S). The authors thank A. Chan and J. Hegemann for thoughtful comments on the manuscript.
The authors declare no competing financial interests.
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Giessen, T., Silver, P. Widespread distribution of encapsulin nanocompartments reveals functional diversity. Nat Microbiol 2, 17029 (2017). https://doi.org/10.1038/nmicrobiol.2017.29
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