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Related Concept Videos

Ribozymes02:47

Ribozymes

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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.
Ribozymes can...
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Bacterial RNA Polymerase00:43

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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.
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Types of RNA01:23

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Three main types of RNA are involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). These RNAs perform diverse functions and can be broadly classified as protein-coding or non-coding RNA. Non-coding RNAs play important roles in the regulation of gene expression in response to developmental and environmental changes. Non-coding RNAs in prokaryotes can be manipulated to develop more effective antibacterial drugs for human or animal use.
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Restriction Enzymes01:11

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Restriction enzymes are bacterial enzymes used to cut DNA in a sequence-specific manner. To cleave DNA, they bind to specific palindromic sequences called restriction sites. Such palindromic DNA sequences or inverted repeats are commonly found in regions of functional significance, such as the origin of replication, gene operator sites, and regions containing transcription termination signals.
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Nucleic Acid Structure01:25

Nucleic Acid Structure

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The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms  a 5′ to 3′ phosphodiester linkage.
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Eukaryotic RNA Polymerases00:58

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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.
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Related Experiment Video

Updated: Oct 3, 2025

Author Spotlight: Characterizing Novel Enzymes from Extremophiles and Common Pathogens to Understand DNA Repair and Replication
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Author Spotlight: Characterizing Novel Enzymes from Extremophiles and Common Pathogens to Understand DNA Repair and Replication

Published on: July 5, 2024

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Structural and Functional Differences between Homologous Bacterial Ribonucleases.

Vera Ulyanova1, Alsu Nadyrova1, Elena Dudkina1

  • 1Department of Microbiology, Institute of Fundamental Medicine and Biology, Kazan (Volga Region) Federal University, 420008 Kazan, Russia.

International Journal of Molecular Sciences
|February 15, 2022
PubMed
Summary

Bacillus ribonucleases (RNases) show subtle structural differences that impact their catalytic activity and interactions with barstar. These variations highlight how minor structural changes can significantly affect protein function and stability.

Keywords:
balifasebalnasebarnasebarstarbinasecatalytic activityribonucleaseribonuclease inhibitorstructural organization

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Kinetic Screening of Nuclease Activity using Nucleic Acid Probes
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Kinetic Screening of Nuclease Activity using Nucleic Acid Probes

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Area of Science:

  • Enzymology
  • Protein Structure-Function Relationships
  • Biochemistry

Background:

  • Bacillus species produce small cationic guanyl-preferring ribonucleases (RNases) with conserved tertiary structures.
  • These homologous RNases form dimers with varying conformations and stability.
  • Understanding functional distinctions among these related enzymes is crucial.

Purpose of the Study:

  • To investigate differences in catalytic activity of homologous RNases towards various RNA substrates.
  • To examine the interaction variations between homologous RNases and the inhibitor protein barstar.
  • To correlate observed functional differences with specific structural features.

Main Methods:

  • Circular dichroism (CD) and dynamic light scattering (DLS) for structural analysis.
  • Spectrometric assays to measure hydrolysis of natural RNA substrates.
  • Stopped-flow kinetic studies using model RNA substrates.
  • Assays to determine inhibition efficiency by barstar.

Main Results:

  • CD and DLS revealed structural distinctions among homologous RNases.
  • RNase activity on natural substrates was similar (high-polymeric RNA > tRNA > dsRNA).
  • Cleavage rates on model RNA substrates and barstar inhibition efficiency varied significantly between homologous RNases.

Conclusions:

  • Homologous Bacillus RNases exhibit distinct catalytic activities and barstar binding efficiencies despite sequence similarity.
  • Minor structural variations in these homologous proteins can lead to significant differences in molecular stability and functional properties.
  • Structure-function relationships in RNases are sensitive to subtle structural modifications.