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

28.2K
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...
28.2K
Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

11.1K
11.1K
Transcription Initiation01:47

Transcription Initiation

22.2K
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...
22.2K
Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

33.9K
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...
33.9K
Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

14.3K
14.3K
The Replisome03:01

The Replisome

39.8K
DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with...
39.8K

You might also read

Related Articles

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

Sort by
Same author

Using Solution NMR to Characterize Biomolecular Condensates Under Biphasic Conditions.

Journal of visualized experiments : JoVE·2026
Same author

Characterization of flexible RNA binding by tandem RNA recognition motifs through integrative ensemble modelling.

Nucleic acids research·2026
Same author

Genome anchoring, retention, and release by neck proteins of Staphylococcus phage 812.

Communications biology·2026
Same author

Development of [<sup>18</sup>F]ACI-19626 as a first-in-class brain PET tracer for imaging TDP-43 pathology.

Nature communications·2025
Same author

A single dose of a vectorized mAb targeting TDP-43 potently inhibits the neuropathology in a model of ALS/FTD.

Molecular therapy : the journal of the American Society of Gene Therapy·2025
Same author

High-throughput screen of 100 000 small molecules in C9ORF72 ALS neurons identifies spliceosome modulators that mobilize G4C2 repeat RNA into nuclear export and repeat associated non-canonical translation.

Nucleic acids research·2025
Same journal

Clinical Europium fluorescent based lectin assays for mucin O-glycomics.

Methods in enzymology·2026
Same journal

A dual-color FRET assay for detection and quantitative analysis of O-glycopeptidases.

Methods in enzymology·2026
Same journal

Evolutionary genetic approaches to analyze mucins.

Methods in enzymology·2026
Same journal

Ex vivo imaging and enzymatic analysis of intestinal mucus.

Methods in enzymology·2026
Same journal

Glyco-TRAPP: A real-time glycocalyx permeability assay for assessing transmembrane mucin barrier function in live and fixed tissues.

Methods in enzymology·2026
Same journal

Quantitative imaging approaches to capture structural and functional dynamics of colonic mucus in health and disease in situ.

Methods in enzymology·2026
See all related articles

Related Experiment Video

Updated: Apr 10, 2026

Genome-wide Surveillance of Transcription Errors in Eukaryotic Organisms
09:30

Genome-wide Surveillance of Transcription Errors in Eukaryotic Organisms

Published on: September 13, 2018

10.1K

One, Two, Three, Four! How Multiple RRMs Read the Genome Sequence.

Tariq Afroz1, Zuzana Cienikova1, Antoine Cléry1

  • 1Institute of Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland.

Methods in Enzymology
|June 13, 2015
PubMed
Summary
This summary is machine-generated.

RNA recognition motifs (RRMs) bind RNA through diverse structural strategies. High-resolution structures reveal how RRMs recognize specific RNA sequences and motifs, aiding in understanding RNA-protein interactions.

Keywords:
CLIPNMRProteinRNARNA recognitionRNA-binding domainRNA–protein complexRRMSELEXStructure

More Related Videos

DNA-Tethered RNA Polymerase for Programmable In vitro Transcription and Molecular Computation
09:26

DNA-Tethered RNA Polymerase for Programmable In vitro Transcription and Molecular Computation

Published on: December 29, 2021

5.0K
Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

7.2K

Related Experiment Videos

Last Updated: Apr 10, 2026

Genome-wide Surveillance of Transcription Errors in Eukaryotic Organisms
09:30

Genome-wide Surveillance of Transcription Errors in Eukaryotic Organisms

Published on: September 13, 2018

10.1K
DNA-Tethered RNA Polymerase for Programmable In vitro Transcription and Molecular Computation
09:26

DNA-Tethered RNA Polymerase for Programmable In vitro Transcription and Molecular Computation

Published on: December 29, 2021

5.0K
Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

7.2K

Area of Science:

  • Structural Biology
  • Molecular Biology
  • Biochemistry

Background:

  • RNA-binding proteins containing RNA recognition motifs (RRMs) are crucial for RNA metabolism.
  • Understanding RRM-RNA interactions is key to deciphering gene regulation.
  • Structural studies of RRMs have been ongoing for over two decades.

Purpose of the Study:

  • To elucidate the structural basis of RRM-mediated RNA recognition.
  • To explain the diverse strategies RRMs employ to bind RNA sequences.
  • To correlate structural findings with genome-wide identified RNA motifs.

Main Methods:

  • High-resolution structural analysis of single and multi RRM-RNA complexes.
  • Analysis of structural variations in RRM folds and tandem RRM arrangements.
  • Comparison of structurally identified RNA motifs with consensus sequences.

Main Results:

  • Multiple RRM fold variations enable specific binding to diverse single-stranded RNA sequences with varying affinities.
  • Tandem RRMs and higher-order ribonucleoprotein complexes (RNPs) exhibit distinct structural arrangements impacting RNA binding.
  • High-resolution structures accurately identify specific RNA motifs bound by RRMs, often matching genome-wide consensus sequences.

Conclusions:

  • Structural insights provide a detailed understanding of RRM-RNA recognition mechanisms.
  • The findings facilitate the prediction of RNA recognition codes for RRMs.
  • Integrating structural and cellular biology advances the comprehension of RRM functions in RNA regulation.