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tRNA Activation02:26

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The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
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Related Experiment Video

Updated: Feb 4, 2026

In vitro tRNA Methylation Assay with the Entamoeba histolytica DNA and tRNA Methyltransferase Dnmt2 Ehmeth Enzyme
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Structural insight into precursor tRNA processing by yeast ribonuclease P.

Pengfei Lan1, Ming Tan2,3, Yuebin Zhang4

  • 1Shanghai Institute of Precision Medicine, Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200125, China.

Science (New York, N.Y.)
|September 29, 2018
PubMed
Summary
This summary is machine-generated.

Ribonuclease P (RNase P), a crucial enzyme, was structurally analyzed alone and with pre-tRNA. Its hook-shaped protein guided by anchors stabilizes the RNA, enabling pre-tRNA processing.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Ribonuclease P (RNase P) is a vital ribozyme essential for tRNA maturation.
  • It processes the 5'-leader sequence of precursor tRNA (pre-tRNA).
  • Understanding its mechanism is key to tRNA biogenesis.

Purpose of the Study:

  • To determine the cryo-electron microscopy structures of Saccharomyces cerevisiae RNase P.
  • To elucidate the structural basis of pre-tRNA binding and catalysis.
  • To provide a molecular understanding of eukaryotic RNase P function.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) at 3.5 angstrom resolution.
  • Structural analysis of RNase P alone and in complex with pre-tRNAPhe.
  • Molecular dynamics simulations to investigate the reaction pathway.

Main Results:

  • The protein components of yeast RNase P form a hook-shaped structure that binds pre-tRNA.
  • This structure acts as a 'measuring device' with anchors recognizing the L-shaped pre-tRNA.
  • Catalytic magnesium ions are coordinated by conserved RNA elements and the pre-tRNA substrate, with substrate binding inducing conformational changes.

Conclusions:

  • The study reveals the detailed architecture of yeast RNase P and its interaction with pre-tRNA.
  • A molecular mechanism involving a two-metal-ion SN2 pathway for pre-tRNA cleavage is proposed.
  • These findings offer insights into the processing of pre-tRNA by eukaryotic RNase P.