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Ribosomes01:27

Ribosomes

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Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
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Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
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Structural Insights into Mdn1, an Essential AAA Protein Required for Ribosome Biogenesis.

Zhen Chen1, Hiroshi Suzuki2, Yuki Kobayashi3

  • 1Laboratory of Chemistry and Cell Biology, The Rockefeller University, New York, NY 10065, USA.

Cell
|October 16, 2018
PubMed
Summary
This summary is machine-generated.

Mdn1, an essential ATPase, releases ribosomal assembly factors. Structural studies reveal how its MIDAS domain docks onto the AAA ring, facilitating factor release during 60S subunit biogenesis.

Keywords:
60S subunitAAA proteinMIDAS domainchemical inhibitordynein-like proteinmidasinribosome biogenesisribozinoindolesingle-particle cryo-EM structure

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Mdn1 is a large AAA-ATPase crucial for ribosome biogenesis.
  • Its function in remodeling ribosomal precursors is poorly understood due to its size and limited homology.
  • Understanding Mdn1's mechanism is key to deciphering ribosome assembly.

Purpose of the Study:

  • To elucidate the structural basis of Mdn1's remodeling function.
  • To investigate how Mdn1 interacts with ribosomal precursors and releases assembly factors.
  • To understand the role of Mdn1's unique domains in its ATPase activity.

Main Methods:

  • X-ray crystallography was used to determine the structures of S. pombe Mdn1.
  • Structures were obtained in the presence of AMPPNP and ATP with the inhibitor Rbn1.
  • Cryo-EM was employed to achieve high-resolution structural data.

Main Results:

  • The structures reveal Mdn1's MIDAS domain is linked to its AAA ring via a long structured linker and a flexible motif.
  • The MIDAS domain docks onto the AAA ring in a nucleotide-dependent manner.
  • Conformational changes in the AAA ring are transmitted to the MIDAS domain, driving factor release.

Conclusions:

  • Mdn1 utilizes a unique structural mechanism involving its MIDAS and AAA domains to release ribosome assembly factors.
  • Nucleotide binding and conformational changes in the AAA ring regulate the interaction of the MIDAS domain.
  • This study provides critical insights into the molecular machinery of ribosomal 60S subunit biogenesis.