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Related Concept Videos

Ribozymes02:47

Ribozymes

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.
Ribozymes can be...
Ribozymes02:47

Ribozymes

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.
Ribozymes can be...
Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
All three eukaryotic RNAPs require specific transcription factors, of which the...
Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
All three eukaryotic RNAPs require specific transcription factors, of which the...
Transcription Initiation01:47

Transcription Initiation

Initiation is the first step of transcription in eukaryotes. Prokaryotic RNA Polymerase (RNAP) can bind to the template DNA and start transcribing. On the other hand, transcription in eukaryotes requires additional proteins, called transcription factors, to first bind to the promoter region in the DNA template. This binding helps recruit the specific RNAP that can assemble on the DNA and start transcription.
The promoters and enhancers and their accessory proteins allow tight regulation of...
Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...

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Related Experiment Video

Updated: Jul 13, 2026

Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro
09:16

Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro

Published on: May 3, 2014

RNase P RNA mediated cleavage: substrate recognition and catalysis.

Leif A Kirsebom1

  • 1Department of Cell and Molecular Biology, Box 596, Biomedical Centre, SE-751 24 Uppsala, Sweden. leif.kirsebom@icm.uu.se

Biochimie
|July 13, 2007
PubMed
Summary

Endoribonuclease P (RNase P) is a crucial enzyme for processing cellular RNA, particularly tRNA precursors. Its catalytic activity resides in the RNA component, conserved across evolution, enabling substrate binding and cleavage.

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Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • RNA Catalysis

Background:

  • Endoribonuclease P (RNase P) is a universally conserved enzyme essential for RNA processing.
  • It comprises an RNA subunit and variable protein subunits, with tRNA precursors as preferred substrates.
  • RNase P's catalytic activity is primarily attributed to its RNA component, independent of protein subunits in vitro.

Purpose of the Study:

  • To review the RNA component of RNase P.
  • To emphasize the current understanding of interactions between RNase P RNA and its substrate.
  • To discuss advancements in understanding substrate binding and catalysis.

Main Methods:

  • Literature review of RNase P structure and function.
  • Analysis of studies on residue contributions to binding and catalysis.
  • Examination of available crystal structures of bacterial RNase P RNA.

Main Results:

  • RNase P RNA possesses inherent catalytic activity, conserved throughout evolution.
  • Significant progress has been made in identifying key residues and chemical groups involved in substrate binding and catalysis.
  • Crystal structures of bacterial RNase P RNA provide insights, though a structure of the RNA-substrate complex is still lacking.

Conclusions:

  • The RNA subunit of RNase P is the catalytic core, demonstrating evolutionary conservation of RNA-based catalysis.
  • Recent structural and biochemical data enhance the understanding of RNase P RNA-substrate interactions.
  • Further research is needed to elucidate the structure of RNase P RNA in complex with its substrate and protein subunits.