1. Nuclear pore-like structures in a compartmentalized bacterium
- Author
-
Garry Morgan, Benjamin K. Yee, Evgeny Sagulenko, Anthony M. Poole, Kathryn Green, Stinus Lindgreen, Ryan J. Catchpole, Richard I. Webb, Nicholas Chia, John A. Fuerst, Kuo-Chang Lee, Andrew Leis, Margaret K. Butler, Uyen Thi Phuong Pham, and Amanda Nouwens
- Subjects
Models, Molecular ,Proteomics ,Protein Structure Comparison ,0301 basic medicine ,Proteome ,Protein Conformation ,Membrane Protein Complexes ,Cell Membranes ,lcsh:Medicine ,Protein Structure Prediction ,Negative Staining ,Biochemistry ,Homology (biology) ,Protein structure ,0302 clinical medicine ,Cell Wall ,Cell Compartmentation ,Macromolecular Structure Analysis ,Fractionation ,Nuclear pore ,lcsh:Science ,Staining ,0303 health sciences ,Multidisciplinary ,biology ,Chemistry ,Planctomycetes ,Eukaryota ,Biological Evolution ,Cell biology ,Membrane Staining ,Separation Processes ,medicine.anatomical_structure ,Membrane ,Eukaryote ,Cellular Structures and Organelles ,Research Article ,Protein Structure ,030106 microbiology ,Research and Analysis Methods ,03 medical and health sciences ,Imaging, Three-Dimensional ,Bacterial Proteins ,Nuclear Membrane ,medicine ,Nuclear membrane ,Molecular Biology ,030304 developmental biology ,Cell Nucleus ,Bacteria ,lcsh:R ,Computational Biology ,Biology and Life Sciences ,Proteins ,Membrane Proteins ,Protein Complexes ,Intracellular Membranes ,Cell Biology ,Internal cell ,biology.organism_classification ,Planctomycetales ,030104 developmental biology ,Specimen Preparation and Treatment ,Nuclear Pore ,Biophysics ,lcsh:Q ,Nucleus ,030217 neurology & neurosurgery - Abstract
Planctomycetes are distinguished from other Bacteria by compartmentalization of cells via internal membranes, interpretation of which has been subject to recent debate regarding potential relations to Gram-negative cell structure. In our interpretation of the available data, the planctomycete Gemmata obscuriglobus contains a nuclear body compartment, and thus possesses a type of cell organization with parallels to the eukaryote nucleus. Here we show that pore-like structures occur in internal membranes of G.obscuriglobus and that they have elements structurally similar to eukaryote nuclear pores, including a basket, ring-spoke structure, and eight-fold rotational symmetry. Bioinformatic analysis of proteomic data reveals that some of the G. obscuriglobus proteins associated with pore-containing membranes possess structural domains found in eukaryote nuclear pore complexes. Moreover, immuno-gold labelling demonstrates localization of one such protein, containing a β-propeller domain, specifically to the G. obscuriglobus pore-like structures. Finding bacterial pores within internal cell membranes and with structural similarities to eukaryote nuclear pore complexes raises the dual possibilities of either hitherto undetected homology or stunning evolutionary convergence.
- Published
- 2016