Direct visualization of translational GTPase factor pool formed around the archaeal ribosomal P-stalk by high-speed AFM.
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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.
- PNAS 117, 32386–32394 (2020). doi: 10.1073/pnas.2018975117
|Kanazawa University (KU), Japan||0.67|
|Niigata University, Japan||0.33|