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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.
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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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Miyazaki
Japan
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Kanazawa-university
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Factor-pooling by ribosomes caught on video using state-of-art high-speed atomic force microscopy technology.
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.
Ribosomes were first discovered in the 1950s and their broad function has been widely understood for some time – they read messenger RNA sequences and from that generate sequences of correctly ordered amino acids into new proteins. The ribosome stalk protein in particular plays an integral role in the protein synthesis process by recruiting protein factors responsible for translation and elongation of the amino acid sequence. How
Japan
Hirotatsu-imai
Toshio-uchiumi
Noriyuki-kodera
Toshio-ando
Proceedings-of-the-national-academy-sciences
Kanazawa-university
Noriyuki-kodera-at-kanazawa-university
Toshio-uchiumi-at-niigata-university
Niigata-university
National-academy
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IMAGE: Structural and dynamic features of three IDPs (N
TAIL, PNT and Sic1) revealed by HS-AFM imaging.
The top and bottom panels correspond to the more-ordered and less ordered states, respectively. The numbers. view more
Credit: Kanazawa University
Our understanding of biological proteins does not always correlate with how common or important they are. Half of all proteins, molecules that play an integral role in cell processes, are intrinsically disordered, which means many of the standard techniques for probing biomolecules don t work on them. Now researchers at Kanazawa University in Japan have shown that their home-grown high-speed atomic force microscopy technology can provide information not just on the structures of these proteins but also their dynamics.
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Kanazawa-university
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