Nuclear Pore-Like Structures in a Compartmentalized Bacterium

PLoS One. 2017 Feb 1;12(2):e0169432. doi: 10.1371/journal.pone.0169432. eCollection 2017.

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, immunogold 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.

MeSH terms

  • Bacteria / metabolism
  • Bacteria / ultrastructure*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Biological Evolution
  • Cell Compartmentation
  • Cell Wall / metabolism
  • Computational Biology / methods
  • Eukaryota / ultrastructure
  • Imaging, Three-Dimensional
  • Intracellular Membranes / ultrastructure
  • Models, Molecular
  • Nuclear Pore / ultrastructure*
  • Planctomycetales / ultrastructure
  • Protein Conformation
  • Proteome
  • Proteomics

Substances

  • Bacterial Proteins
  • Proteome

Grants and funding

JAF was supported by Australian Research Council Discovery Project DP0881485. AMP was supported by Royal Society of New Zealand RDF-UOC1101. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.