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

Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

13.3K
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,...
13.3K
Rab Cascades01:25

Rab Cascades

2.7K
Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
2.7K
RNA Interference01:23

RNA Interference

26.1K
RNA interference (RNAi) is a process in which a small non-coding RNA molecule blocks the post-transcriptional expression of a gene by binding to its messenger RNA (mRNA) and preventing the protein from being translated.
This process occurs naturally in cells, often through the activity of genomically-encoded microRNAs. Researchers can take advantage of this mechanism by introducing synthetic RNAs to deactivate specific genes for research or therapeutic purposes. For example, RNAi could be used...
26.1K
Rab Proteins01:14

Rab Proteins

4.0K
Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
4.0K
siRNA - Small Interfering RNAs02:30

siRNA - Small Interfering RNAs

16.9K
Small interfering RNAs, or siRNAs, are short regulatory RNA molecules that can silence genes post-transcriptionally, as well as the transcriptional level in some cases. siRNAs are important for protecting cells against viral infections and silencing transposable genetic elements.
In the cytoplasm, siRNA is processed from a double-stranded RNA, which comes from either endogenous DNA transcription or exogenous sources like a virus. This double-stranded RNA is then cleaved by the...
16.9K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

7.3K
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
7.3K

You might also read

Related Articles

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

Sort by
Same author

Reversible DNA condensation drives natural transformation.

Nature communications·2026
Same author

ComFB, a widespread family of c-di-NMP receptor proteins.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Reversible DNA condensation drives natural transformation.

bioRxiv : the preprint server for biology·2025
Same author

c-di-GMP-Dependent Regulation of Motility by <i>comFB</i> and <i>comFC</i>.

bioRxiv : the preprint server for biology·2025
Same author

ComFB, a new widespread family of c-di-NMP receptor proteins.

bioRxiv : the preprint server for biology·2024
Same author

Formation of a stable RNase Y-RicT (YaaT) complex requires RicA (YmcA) and RicF (YlbF).

mBio·2023

Related Experiment Video

Updated: Jul 27, 2025

Identification of Footprints of RNA:Protein Complexes via RNA Immunoprecipitation in Tandem Followed by Sequencing RIPiT-Seq
09:26

Identification of Footprints of RNA:Protein Complexes via RNA Immunoprecipitation in Tandem Followed by Sequencing RIPiT-Seq

Published on: July 10, 2019

10.6K

Formation of a stable RNase Y-RicT (YaaT) complex requires RicA (YmcA) and RicF (YlbF).

Eugenie Dubnau1, Micaela DeSantis1, David Dubnau1,2

  • 1Public Health Research Institute, Rutgers University, 225 Warren Street, Newark, New Jersey, 07103, USA.

Biorxiv : the Preprint Server for Biology
|June 9, 2023
PubMed
Summary

In Bacillus subtilis, RNase Y (Rny) interacts with the RicT protein, forming a complex essential for stabilizing key metabolic transcripts. This interaction requires the RicA and RicF proteins and is crucial for gapA mRNA maturation.

More Related Videos

A Simple Fluorescence-based Reporter Assay to Identify Cellular Components Required for Ricin Toxin A Chain RTA Trafficking in Yeast
09:03

A Simple Fluorescence-based Reporter Assay to Identify Cellular Components Required for Ricin Toxin A Chain RTA Trafficking in Yeast

Published on: December 15, 2017

8.1K
Capture and Identification of RNA-binding Proteins by Using Click Chemistry-assisted RNA-interactome Capture CARIC Strategy
09:36

Capture and Identification of RNA-binding Proteins by Using Click Chemistry-assisted RNA-interactome Capture CARIC Strategy

Published on: October 19, 2018

9.4K

Related Experiment Videos

Last Updated: Jul 27, 2025

Identification of Footprints of RNA:Protein Complexes via RNA Immunoprecipitation in Tandem Followed by Sequencing RIPiT-Seq
09:26

Identification of Footprints of RNA:Protein Complexes via RNA Immunoprecipitation in Tandem Followed by Sequencing RIPiT-Seq

Published on: July 10, 2019

10.6K
A Simple Fluorescence-based Reporter Assay to Identify Cellular Components Required for Ricin Toxin A Chain RTA Trafficking in Yeast
09:03

A Simple Fluorescence-based Reporter Assay to Identify Cellular Components Required for Ricin Toxin A Chain RTA Trafficking in Yeast

Published on: December 15, 2017

8.1K
Capture and Identification of RNA-binding Proteins by Using Click Chemistry-assisted RNA-interactome Capture CARIC Strategy
09:36

Capture and Identification of RNA-binding Proteins by Using Click Chemistry-assisted RNA-interactome Capture CARIC Strategy

Published on: October 19, 2018

9.4K

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Microbiology

Background:

  • Nucleases play a vital role in RNA processing, essential for generating mature transcripts in all life forms.
  • In Bacillus subtilis, RNase Y (Rny) and the Ric proteins (RicA, RicF, RicT) are crucial for cleaving and stabilizing transcripts involved in intermediary metabolism, including glycolysis and oxidative phosphorylation.
  • These proteins and their regulatory mechanisms are conserved in firmicutes, including pathogens, highlighting their biological significance.

Approach:

  • Investigated the interactions between RNase Y (Rny) and the Ric proteins (RicA, RicF, RicT) in Bacillus subtilis.
  • Determined the specific binding partners of Rny within the Ric complex.
  • Utilized biochemical assays to confirm the formation and requirements of the Rny-RicT complex and the role of iron-sulfur clusters.

Key Points:

  • RicT, but not RicA or RicF alone, forms a stable complex with RNase Y (Rny).
  • The formation of the Rny-RicT complex is dependent on the presence of RicA and RicF, suggesting RicT is transferred from a ternary Ric complex to Rny.
  • The two iron-sulfur clusters within the ternary Ric complex are essential for the stable association between RicT and Rny.

Conclusions:

  • RNase Y (Rny) engages in distinct RNA processing activities based on its binding partners.
  • A stable complex between RicT and Rny is likely the active form responsible for the maturation of gapA mRNA.
  • Proteins of the degradosome-like network interacting with Rny are not essential for gapA operon processing, indicating specialized roles for Rny.