Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Bacterial RNA Polymerase

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...

Bacterial RNA Polymerase

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...

Bacterial Transcription

Bacterial Transcription

RNA polymerase (RNAP) carries out DNA-dependent RNA synthesis in both bacteria and eukaryotes. Bacteria do not have a membrane-bound nucleus. So, transcription and translation occur simultaneously, on the same DNA template.
Transcription can be divided into three main stages, each involving distinct DNA sequences to guide the polymerase. These are:

Eukaryotic RNA Polymerases

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 Polymerases

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 Initiation

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Preparation and properties of copper-oil-based nanofluids.

Nanoscale research letters·2011

Same author

Ordered gelation of chemically converted graphene for next-generation electroconductive hydrogel films.

Angewandte Chemie (International ed. in English)·2011

Same author

Stereoselective synthesis of highly substituted enamides by an oxidative Heck reaction.

Angewandte Chemie (International ed. in English)·2011

Same author

A highly selective and sensitive on-off sensor for silver ions and cysteine by light scattering technique of DNA-functionalized gold nanoparticles.

Chemical communications (Cambridge, England)·2011

Same author

The remarkable enhancement of CO-pretreated CuO-Mn2O3/γ-Al2O3 supported catalyst for the reduction of NO with CO: the formation of surface synergetic oxygen vacancy.

Chemistry (Weinheim an der Bergstrasse, Germany)·2011

Same author

Application of multiwall carbon nanotubes-based matrix solid phase dispersion extraction for determination of hormones in butter by gas chromatography mass spectrometry.

Journal of chromatography. A·2011

Search research articles

Related Experiment Video

Updated: Jun 2, 2026

Chemical Triphosphorylation of Oligonucleotides

Chemical Triphosphorylation of Oligonucleotides

Published on: June 2, 2022

Archaeal-bacterial chimeric RNase P RNAs: towards understanding RNA's architecture, function and evolution.

Dan Li¹, Markus Gössringer, Roland K Hartmann

¹Institut für Biochemie, Justus-Liebig-Universität Giessen, Giessen, Germany.

Chembiochem : a European Journal of Chemical Biology

|May 17, 2011

Summary

Archaeal RNase P RNA catalytic domains can replace bacterial counterparts in E. coli. This adaptation highlights conserved RNA structures and evolved protein interactions in ribonuclease P evolution.

More Related Videos

Computational Analysis Tutorial for Chimeric Small Noncoding RNA: Target RNA Sequencing Libraries

Computational Analysis Tutorial for Chimeric Small Noncoding RNA: Target RNA Sequencing Libraries

Published on: December 1, 2023

Related Experiment Videos

Last Updated: Jun 2, 2026

Chemical Triphosphorylation of Oligonucleotides

Chemical Triphosphorylation of Oligonucleotides

Published on: June 2, 2022

Computational Analysis Tutorial for Chimeric Small Noncoding RNA: Target RNA Sequencing Libraries

Computational Analysis Tutorial for Chimeric Small Noncoding RNA: Target RNA Sequencing Libraries

Published on: December 1, 2023

Area of Science:

Molecular Biology
Evolutionary Biology
Biochemistry

Background:

Archaeal RNase P has higher protein content and lower RNA-alone activity than bacterial RNase P.
RNase P is essential for cell viability, catalyzing precursor tRNA maturation.

Purpose of the Study:

To investigate the functional interchangeability of archaeal and bacterial RNase P RNA catalytic domains.
To understand the structural and evolutionary adaptations in RNase P RNA.

Main Methods:

Construction of a chimeric P RNA combining archaeal and bacterial RNase P RNA domains.
Functional assessment of the chimeric P RNA in Escherichia coli cells.
Analysis of structural modifications and interdomain contacts required for function.

Main Results:

An archaeal RNase P RNA catalytic domain, with specific alterations, functionally replaced the E. coli catalytic domain.
Restoration of L9-P1 and introduction of L18-P8 interdomain contacts were crucial for chimeric P RNA function.
Chimeric P RNA exhibited reduced cellular levels in E. coli, necessitating protein overexpression.

Conclusions:

The catalytic domains of type A bacterial and archaeal P RNAs are largely conserved evolutionarily.
Archaeal RNase P likely evolved protein-protein contacts to replace the L18-P8 RNA-RNA interaction.
Functional complementation demonstrates conserved RNA structure and highlights divergent evolutionary paths in RNase P.