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

Transfer RNA Synthesis02:36

Transfer RNA Synthesis

11.9K
One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
11.9K
Pre-mRNA Processing: Modification of pre-mRNA Ends01:35

Pre-mRNA Processing: Modification of pre-mRNA Ends

9.3K
In eukaryotic cells, transcripts made by RNA polymerase are modified and processed before exiting the nucleus. Unprocessed RNA is called precursor mRNA or pre-mRNA to distinguish it from mature mRNA.
Once about 20-40 ribonucleotides have been joined together by RNA polymerase, a group of enzymes adds a cap to the 5' end of the growing transcript. In this process, a 5' phosphate is replaced by modified guanosine that has a methyl group attached (7-methyl guanosine). This 5' cap helps...
9.3K
Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

24.1K
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...
24.1K
pre-mRNA Processing02:01

pre-mRNA Processing

52.8K
In eukaryotic cells, transcripts made by RNA polymerase are modified and processed before exiting the nucleus. Unprocessed RNA is called precursor mRNA or pre-mRNA to distinguish it from mature mRNA.
Once about 20-40 ribonucleotides have been joined together by RNA polymerase, a group of enzymes adds a “cap” to the 5’ end of the growing transcript. In this process, a 5’ phosphate is replaced by modified guanosine that has a methyl group attached to it (7-Methyl...
52.8K
Ribozymes02:47

Ribozymes

11.2K
The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can...
11.2K
Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

13.2K
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,...
13.2K

You might also read

Related Articles

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

Sort by
Same author

Perturbation of the circadian rhythmic transcription contributes to radiotherapy-induced salivary gland hypofunction.

Communications biology·2026
Same author

A framework for the exploration of subcellular compartmentalization of RNA-binding proteins.

Nature communications·2026
Same author

S-phase PARylation of microprotein RSMC enhances the function of Sororin in sister chromatid cohesion.

The EMBO journal·2025
Same author

MCM5 UFMylation regulates replication origin firing and fork progression.

The EMBO journal·2025
Same author

DNA damage response regulator ATR licenses PINK1-mediated mitophagy.

Nucleic acids research·2025
Same author

FOXP1 phosphorylation antagonizes its O-GlcNAcylation in regulating ATR activation in response to replication stress.

The EMBO journal·2024

Related Experiment Video

Updated: Jun 24, 2025

Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro
09:16

Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro

Published on: May 3, 2014

12.8K

RNase P: Beyond Precursor tRNA Processing.

Peipei Wang1, Juntao Lin1,2, Xiangyang Zheng3

  • 1Guangdong Key Laboratory for Genome Stability & Disease Prevention and Marshall Laboratory of Biomedical Engineering, Shenzhen University Medical School, Shenzhen University, Shenzhen 518060, China.

Genomics, Proteomics & Bioinformatics
|June 11, 2024
PubMed
Summary
This summary is machine-generated.

Ribonuclease P (RNase P) is vital for tRNA maturation and also plays roles in DNA repair and genome stability. These non-canonical functions suggest RNase P as a potential therapeutic target for cancer treatment.

Keywords:
Chromatin assemblyDNA damage responseGenome stabilityRNase PTumorigenesis

More Related Videos

Fluorescence Based Primer Extension Technique to Determine Transcriptional Starting Points and Cleavage Sites of RNases In Vivo
10:51

Fluorescence Based Primer Extension Technique to Determine Transcriptional Starting Points and Cleavage Sites of RNases In Vivo

Published on: October 31, 2014

27.1K
Analysis of Termination of Transcription Using BrUTP-strand-specific Transcription Run-on TRO Approach
12:12

Analysis of Termination of Transcription Using BrUTP-strand-specific Transcription Run-on TRO Approach

Published on: March 12, 2017

9.8K

Related Experiment Videos

Last Updated: Jun 24, 2025

Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro
09:16

Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro

Published on: May 3, 2014

12.8K
Fluorescence Based Primer Extension Technique to Determine Transcriptional Starting Points and Cleavage Sites of RNases In Vivo
10:51

Fluorescence Based Primer Extension Technique to Determine Transcriptional Starting Points and Cleavage Sites of RNases In Vivo

Published on: October 31, 2014

27.1K
Analysis of Termination of Transcription Using BrUTP-strand-specific Transcription Run-on TRO Approach
12:12

Analysis of Termination of Transcription Using BrUTP-strand-specific Transcription Run-on TRO Approach

Published on: March 12, 2017

9.8K

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Ribonuclease P (RNase P) traditionally known for tRNA processing.
  • Emerging evidence reveals non-canonical functions beyond RNA catalysis.
  • RNase P's role in cellular processes is increasingly recognized.

Purpose of the Study:

  • Review recent advancements in understanding RNase P's non-canonical functions.
  • Explore RNase P's involvement in chromatin assembly and DNA damage response.
  • Discuss implications for genome stability, tumorigenesis, and cancer therapeutics.

Main Methods:

  • Literature review of recent studies on RNase P.
  • Analysis of research on RNase P's roles in DNA repair and genome maintenance.
  • Synthesis of findings related to cancer biology and therapeutic potential.

Main Results:

  • RNase P participates in chromatin assembly.
  • RNase P is involved in DNA damage response pathways.
  • Dysregulation of RNase P is linked to genome instability and cancer.

Conclusions:

  • RNase P possesses critical non-canonical functions in genome maintenance.
  • RNase P's involvement in tumorigenesis highlights its significance in cancer.
  • RNase P represents a promising therapeutic target for oncological treatments.