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Mycoplasma mobile moves into overdrive: Twin motor modified from ATP synthase discovered
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Twin motor modified from ATP synthase discovered
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VIDEO: The cells are gliding on glass. They always go in the direction of their tapered end with speeds 2 to 4 μm per second. view more
Credit: Yuya Sasajima (Osaka City University)
Much of human invention and innovation has been the result of our discovery and replication of natural phenomena, from birds serving to inspire human flight, to whales allowing us to dive deep into the ocean with submarines. For the first time ever, researchers have captured at the nanometer level the gliding machinery of the bacterium
Mycoplasma mobile. Their findings were published in
mBio. This brings us closer to understanding the origin and operating principle of motility, which could serve as a basis for the next generation of nanoscale devices and pharmaceuticals.
Researchers at Kanazawa University report in the
Journal of Physical Chemistry Letters how high-speed atomic force microscopy can be used for studying DNA wrapping processes. The technique enables visualizing the dynamics of DNA–protein interactions, which in certain cases resembles the motion of inchworms.
The genetic material of most organisms is carried by DNA, a complex organic molecule. DNA is very long for humans, the molecule is estimated to be about 2 m in length. In cells, DNA occurs in a densely packed form, with strands of the molecule coiled up in a complicated but efficient space-filling way. A key role in DNA s compactification is played by histones, structural-support proteins around which a part of a DNA molecule can wrap. The DNA–histone wrapping process is reversible the two molecules can unwrap and rewrap but little is known about the mechanisms at play. Now, by applying high-speed atomic-force microscopy (HS-AFM), Richard Wong and colleagu
Home > Press > High-speed atomic force microscopy visualizes cell protein factories
Model of translating ribosomes and elongation factors. EF1AGTPaatRNA and EF2 assemble to the ribosomal stalk on the translating ribosome. The translation factor pool contributes to efficient protein synthesis in a crowded intracellular environment.
CREDIT
Proceedings of the National Academy of Sciences
Abstract:
Ribosomes are the complexes of ribonucleoproteins at the heart of protein synthesis in cells. However in the absence of conclusive evidence, how these complexes operate has been open to debate. Now Hirotatsu Imai and Noriyuki Kodera at Kanazawa University, alongside Toshio Uchiumi at Niigata University in Japan, show visualizations of the structural dynamics and factor pooling that take place at ribosome stalk proteins as they build new proteins.
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