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

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...
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

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...
Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
piRNA - Piwi-interacting RNAs02:57

piRNA - Piwi-interacting RNAs

PIWI-interacting RNAs, or piRNAs, are the most abundant short non-coding RNAs. More than 20,000 genes have been found in humans that code for piRNAs while only 2000 genes have been found for miRNAs. piRNAs can act at the transcriptional and post-transcriptional levels and have a vital role in silencing transposable elements present in germ cells. They are also involved in epigenetic silencing and activation. Previously, they were thought to function only in germ cells but new evidence suggests...
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

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...

You might also read

Related Articles

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

Sort by
Same author

Reconstruction of septin higher-order nano-size structures in ovarian cancer cells uncover susceptibility to the septin-targeting small molecule UR214-9.

bioRxiv : the preprint server for biology·2026
Same author

Roles for Phosphatase PP4 in Rhythmicity and Compensation in the Neurospora Circadian System.

bioRxiv : the preprint server for biology·2026
Same author

Local delivery of SBRT and IL-12 to murine PDAC tumors modulates hematopoiesis.

Oncoimmunology·2026
Same author

Diverse roles of YTHDC1 in chromatin and blood cancers.

Frontiers in genetics·2026
Same author

Epigenetic Inheritance Through Replication-Coupled Parental Histone Recycling.

Annual review of cell and developmental biology·2026
Same author

ATAD2 mediates chromatin-bound histone chaperone turnover.

eLife·2026

Related Experiment Video

Updated: Jul 8, 2026

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution
10:53

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution

Published on: January 16, 2017

Two RNAi complexes, RITS and RDRC, physically interact and localize to noncoding centromeric RNAs.

Mohammad R Motamedi1, André Verdel, Serafin U Colmenares

  • 1Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.

Cell
|December 21, 2004
PubMed
Summary

RNA-directed RNA polymerase complex (RDRC) physically and functionally links with the RNA-induced transcriptional silencing (RITS) complex. This interaction is crucial for siRNA-dependent heterochromatin assembly in fission yeast.

More Related Videos

Novel RNA-Binding Proteins Isolation by the RaPID Methodology
11:19

Novel RNA-Binding Proteins Isolation by the RaPID Methodology

Published on: September 30, 2016

RNA-Associated Chromatin DNA-DNA Interaction Method
11:01

RNA-Associated Chromatin DNA-DNA Interaction Method

Published on: April 30, 2026

Related Experiment Videos

Last Updated: Jul 8, 2026

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution
10:53

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution

Published on: January 16, 2017

Novel RNA-Binding Proteins Isolation by the RaPID Methodology
11:19

Novel RNA-Binding Proteins Isolation by the RaPID Methodology

Published on: September 30, 2016

RNA-Associated Chromatin DNA-DNA Interaction Method
11:01

RNA-Associated Chromatin DNA-DNA Interaction Method

Published on: April 30, 2026

Area of Science:

  • Epigenetics
  • RNA interference (RNAi)
  • Molecular biology

Background:

  • RNAi-mediated heterochromatin assembly requires the RITS complex and Rdp1.
  • The precise function and interactions of Rdp1 in this process were not fully understood.

Purpose of the Study:

  • To elucidate the molecular interactions and functional significance of Rdp1 in heterochromatin assembly.
  • To characterize the complex formed by Rdp1 and its associated proteins.

Main Methods:

  • Co-immunoprecipitation to identify interacting protein complexes.
  • Analysis of protein localization using microscopy.
  • siRNA profiling in knockout strains.
  • Assays for RNA-directed RNA polymerase activity.

Main Results:

  • Rdp1 forms a complex (RDRC) with Hrr1 (RNA helicase) and Cid12 (polyA polymerase) with RNA-directed RNA polymerase activity.
  • RDRC interacts with RITS, requiring Dicer (Dcr1) and Clr4.
  • Both RDRC and RITS localize to the nucleus and associate with centromeric RNAs in a Dcr1-dependent manner.
  • Loss of Rdp1, Hrr1, or Cid12 results in RITS lacking siRNAs and failing to localize to centromeric repeats.

Conclusions:

  • A physical and functional link exists between Rdp1 and the RITS complex.
  • Noncoding RNAs serve as a platform for siRNA-dependent localization of RNAi machinery to specific genomic regions.
  • This study reveals a novel mechanism for heterochromatin formation mediated by RNA-directed RNA polymerase activity and RITS.