Morphology of the archaellar motor and associated cytoplasmic cone in Thermococcus kodakaraensis

EMBO Rep. 2017 Sep;18(9):1660-1670. doi: 10.15252/embr.201744070. Epub 2017 Jul 19.

Abstract

Archaeal swimming motility is driven by archaella: rotary motors attached to long extracellular filaments. The structure of these motors, and particularly how they are anchored in the absence of a peptidoglycan cell wall, is unknown. Here, we use electron cryotomography to visualize the archaellar basal body in vivo in Thermococcus kodakaraensis KOD1. Compared to the homologous bacterial type IV pilus (T4P), we observe structural similarities as well as several unique features. While the position of the cytoplasmic ATPase appears conserved, it is not braced by linkages that extend upward through the cell envelope as in the T4P, but rather by cytoplasmic components that attach it to a large conical frustum up to 500 nm in diameter at its base. In addition to anchoring the lophotrichous bundle of archaella, the conical frustum associates with chemosensory arrays and ribosome-excluding material and may function as a polar organizing center for the coccoid cells.

Keywords: Thermococcus kodakarensis; archaeal motility; archaella; electron cryotomography; flagella.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Archaeal Proteins / metabolism
  • Cell Membrane / metabolism
  • Cell Membrane / ultrastructure
  • Cell Surface Extensions / physiology
  • Cell Surface Extensions / ultrastructure*
  • Cryoelectron Microscopy
  • Cytoplasm / physiology
  • Cytoplasm / ultrastructure*
  • Flagella / physiology
  • Flagella / ultrastructure
  • Thermococcus / cytology
  • Thermococcus / physiology*
  • Thermococcus / ultrastructure*

Substances

  • Archaeal Proteins
  • Adenosine Triphosphatases