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Related Concept Videos

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...
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...
RNA Structure01:19

RNA Structure

The basic structure of RNA consists of a string of ribonucleotides attached by phosphodiester bonds. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
Different Types of RNA Have the Same Basic Structure
There are three main types of ribonucleic acid (RNA) involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). All three...
RNA Structure01:23

RNA Structure

Overview
The basic structure of RNA consists of a five-carbon sugar and one of four nitrogenous bases. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
Different Types of RNA Have the Same Basic Structure
There are three main types of ribonucleic acid (RNA): messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). All three RNA types consist of a...

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Related Experiment Video

Updated: May 11, 2026

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids
09:04

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids

Published on: September 21, 2017

Structural studies of RNase P.

Alfonso Mondragón1

  • 1Department of Molecular Biosciences, Northwestern University, Evanston, Illinois 60208, USA. a-mondragon@northwestern.edu

Annual Review of Biophysics
|May 10, 2013
PubMed
Summary
This summary is machine-generated.

Ribonuclease P (RNase P), a universal ribozyme, processes pre-tRNAs. Structural and biochemical studies reveal its atomic-level mechanism and the evolution of RNA enzymes.

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Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle
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Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle

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Last Updated: May 11, 2026

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids
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Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids

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Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle
10:05

Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle

Published on: March 5, 2019

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Ribonuclease P (RNase P) is a universally conserved ribozyme essential for RNA processing.
  • It catalyzes the maturation of the 5' end of precursor transfer RNAs (pre-tRNAs).
  • RNase P comprises a catalytic RNA component and associated proteins, forming a ribonucleoprotein complex.

Purpose of the Study:

  • To elucidate the atomic-level mechanism of RNase P catalysis.
  • To understand the structural basis of RNA-protein recognition within RNase P.
  • To explore the evolutionary trajectory of enzymes from an RNA-based world.

Main Methods:

  • Structural studies of RNase P proteins from diverse organisms.
  • Analysis of the bacterial RNase P RNA component.
  • X-ray crystallography of a bacterial RNase P holoenzyme/tRNA complex.

Main Results:

  • Provided atomic-level insights into the catalytic mechanism of RNase P.
  • Revealed the structural architecture of the RNase P holoenzyme and its interaction with tRNA.
  • Expanded understanding of large RNA molecule structures and ribonucleoprotein complex assembly.

Conclusions:

  • Structural and biochemical data offer a comprehensive view of RNase P function.
  • These findings deepen our knowledge of ribozyme catalysis and RNA recognition.
  • The study contributes to understanding the evolution of enzymes and the transition to a protein-based world.