Self-sorting of foreign proteins in a bacterial nanocompartment

W.F. Rurup, J. Snijder, M.S.T. Koay, A.J.R. Heck, Jeroen Johannes Lambertus Maria Cornelissen

Research output: Contribution to journalArticleAcademicpeer-review

59 Citations (Scopus)

Abstract

Nature uses bottom-up approaches for the controlled assembly of highly ordered hierarchical structures with defined functionality, such as organelles, molecular motors, and transmembrane pumps. The field of bionanotechnology draws inspiration from nature by utilizing biomolecular building blocks such as DNA, proteins, and lipids, for the (self-) assembly of new structures for applications in biomedicine, optics, or electronics. Among the toolbox of available building blocks, proteins that form cage-like structures, such as viruses and virus-like particles, have been of particular interest since they form highly symmetrical assemblies and can be readily modified genetically or chemically both on the outer or inner surface. Bacterial encapsulins are a class of nonviral protein cages that self-assemble in vivo into stable icosahedral structures. Using teal fluorescent proteins (TFP) engineered with a specific native C-terminal docking sequence, we report the molecular self-sorting and selective packaging of TFP cargo into bacterial encapsulins during in vivo assembly. Using native mass spectrometry techniques, we show that loading of either monomeric or dimeric TFP cargo occurs with unprecedented high fidelity and exceptional loading accuracy. Such self-assembling systems equipped with self-sorting capabilities would open up exciting opportunities in nanotechnology, for example, as artificial (molecular storage or detoxification) organelles or as artificial cell factories for in situ biocatalysis.
Original languageEnglish
Pages (from-to)3828-3832
Number of pages4
JournalJournal of the American Chemical Society
Volume136
Issue number10
DOIs
Publication statusPublished - 2014

Keywords

  • METIS-308362
  • IR-95076

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