Direct visualization of translational GTPase factor pool formed around the archaeal ribosomal P-stalk by high-speed AFM.

Research Highlight

Protein factories of the cell have bendy, tentacle-like arms

© theasis/E+/Getty Images

© theasis/E+/Getty Images

Ribosomes — the protein factories of the cell — use an octopus-like appendage to recruit the molecules they need to make proteins.

The ribosome is one of the best-characterized protein complexes in biology, but researchers have mostly taken static snapshots of the structure.

To obtain a dynamic picture of the ribosome’s changing molecular assembly, a team led by Kanazawa University researchers turned to high-speed atomic force microscopy — an imaging technique capable of visualizing sub-cellular structures at high spatial and temporal resolution.

The team focused on one component of the ribosome called the P-stalk, a flexible, six-part structure with tentacle-like arms that helps recruit molecules needed for protein production.

The movies revealed how the P-stalk latches onto two so-called elongation factors — one involved in bringing protein building blocks to the ribosome, the other in moving protein synthesis along. In this way, the bendy P-stalk maintains a concentrated, localized pool of these factors for efficient ribosome function.

Supported content

  1. PNAS 117, 32386–32394 (2020). doi: 10.1073/pnas.2018975117
Institutions Share
Kanazawa University (KU), Japan 0.67
Niigata University, Japan 0.33

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