Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

27.2K
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...
27.2K
Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

9.6K
9.6K
Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

32.9K
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...
32.9K
Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

12.1K
12.1K
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

11.1K
Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
11.1K
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

4.1K
4.1K

You might also read

Related Articles

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

Sort by
Same author

Virtual screening and molecular fingerprinting for <i>in silico</i> designing of potential CCR5 inhibitors targeting HIV therapy.

Journal of biomolecular structure & dynamics·2026
Same author

Competitive Viral Interference Controls Arbovirus Co-Transmission in Aedes aegypti.

Scientific reports·2025
Same author

A comprehensive review on in vitro therapies for virus elimination and novel methods for virus protection in key horticultural crops.

Planta·2025
Same author

Accessory viral protein, V, of Newcastle Disease Virus binds dsRNA to facilitate immune evasion.

Virusdisease·2025
Same author

Digital framework for georeferenced multiplatform surveillance of banana wilt using human in the loop AI and YOLO foundation models.

Scientific reports·2025
Same author

Geographical Distribution, Host Range and Genetic Diversity of <i>Fusarium oxysporum</i> f. sp. <i>cubense</i> Causing <i>Fusarium</i> Wilt of Banana in India.

Journal of fungi (Basel, Switzerland)·2024
Same journal

Correction: Bulatov et al. Camelpox Virus in Western Kazakhstan: Assessment of the Role of Local Fauna as Reservoirs of Infection. <i>Viruses</i> 2024, <i>16</i>, 1626.

Viruses·2026
Same journal

Correction: Franco et al. Whole Blood Volume-Based Absolute Quantification of HTLV-1 Proviral Load: A Comparative Method Evaluation Study. <i>Viruses</i> 2026, <i>18</i>, 580.

Viruses·2026
Same journal

Correction: Medkour et al. Adenovirus Infections in African Humans and Wild Non-Human Primates: Great Diversity and Cross-Species Transmission. <i>Viruses</i> 2020, <i>12</i>, 657.

Viruses·2026
Same journal

Burden of Malaria and Dengue Across Global, Asian, and Chinese Populations Based on GBD 2021 Data: A Quantitative Assessment of Importation Risks to China.

Viruses·2026
Same journal

First Report of <i>Orthonairovirus songlingense</i> in <i>Haemaphysalis concinna</i> Ticks from Russia.

Viruses·2026
Same journal

Epidemiological and Virological Characteristics of H9N2 Avian Influenza Virus in Jiangsu Province, China, 2024.

Viruses·2026
See all related articles

Related Experiment Video

Updated: Feb 14, 2026

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
10:59

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

Published on: May 13, 2019

10.2K

RNA Dependent RNA Polymerases: Insights from Structure, Function and Evolution.

Sangita Venkataraman1, Burra V L S Prasad2, Ramasamy Selvarajan3

  • 1Department of Biotechnology, Acharya Nagarjuna University, Nagarjuna Nagar, Guntur 522510, India. sangita.venkataraman@gmail.com.

Viruses
|February 15, 2018
PubMed
Summary
This summary is machine-generated.

RNA dependent RNA polymerase (RdRp) enzymes are vital for viral RNA replication and transcription. Their conserved "cupped right hand" structure, involving specific subdomains and metal ions, is key to function and antiviral development.

Keywords:
RNA virusesRNA-dependent RNA polymerasedomainsinhibitor complexesmotifsstructure-based Phylogeny

More Related Videos

Semi-quantitative Detection of RNA-dependent RNA Polymerase Activity of Human Telomerase Reverse Transcriptase Protein
08:26

Semi-quantitative Detection of RNA-dependent RNA Polymerase Activity of Human Telomerase Reverse Transcriptase Protein

Published on: June 12, 2018

10.4K
RNA Secondary Structure Prediction Using High-throughput SHAPE
13:42

RNA Secondary Structure Prediction Using High-throughput SHAPE

Published on: May 31, 2013

32.3K

Related Experiment Videos

Last Updated: Feb 14, 2026

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
10:59

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

Published on: May 13, 2019

10.2K
Semi-quantitative Detection of RNA-dependent RNA Polymerase Activity of Human Telomerase Reverse Transcriptase Protein
08:26

Semi-quantitative Detection of RNA-dependent RNA Polymerase Activity of Human Telomerase Reverse Transcriptase Protein

Published on: June 12, 2018

10.4K
RNA Secondary Structure Prediction Using High-throughput SHAPE
13:42

RNA Secondary Structure Prediction Using High-throughput SHAPE

Published on: May 31, 2013

32.3K

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • RNA dependent RNA polymerase (RdRp) is essential for RNA virus replication and transcription.
  • RdRp enzymes exhibit conserved structural features despite sequence variations.
  • The enzyme's structure resembles a cupped right hand with distinct subdomains.

Purpose of the Study:

  • To provide an overview of the structural aspects of RdRps.
  • To analyze RdRp complexes with substrates, inhibitors, and metal ions.
  • To present a structure-based phylogeny of RdRps from Group III, IV, and V viruses.

Main Methods:

  • Structural analysis of RdRp enzymes and their complexes.
  • Comparative analysis of RdRp structures across different viral groups.
  • Phylogenetic analysis based on structural data.

Main Results:

  • Conserved core structural features of RdRps were identified.
  • The catalytic mechanism involving conserved aspartates and metal ions was elucidated.
  • Structural insights into RdRp complexes offer potential for antiviral drug development.

Conclusions:

  • Structural studies of RdRps provide critical insights into viral replication mechanisms.
  • Understanding RdRp structure-based phylogeny aids in classifying and studying RNA viruses.
  • The conserved structural features of RdRp are crucial targets for antiviral strategies.