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

RNA Splicing01:32

RNA Splicing

61.8K
Splicing is the process by which eukaryotic RNA is edited before its translation into protein. The RNA strand transcribed from eukaryotic DNA is called the primary transcript. The primary transcripts that become mRNAs are called precursor messenger RNAs (pre-mRNAs). Eukaryotic pre-mRNA contains alternating sequences of exons and introns. Exons are nucleotide sequences that code for proteins, whereas introns are the non-coding regions. In RNA splicing, introns are removed and exons are bonded...
61.8K
RNA Splicing01:32

RNA Splicing

20.5K
20.5K
Termination of Translation01:44

Termination of Translation

28.9K
The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
28.9K
Leaky Scanning02:28

Leaky Scanning

5.9K
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
5.9K
Pre-mRNA Processing: Modification of pre-mRNA Ends01:35

Pre-mRNA Processing: Modification of pre-mRNA Ends

18.0K
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...
18.0K
pre-mRNA Processing02:01

pre-mRNA Processing

58.8K
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...
58.8K

You might also read

Related Articles

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

Sort by
Same author

Author Correction: Structural basis for translational control by the human 48S initiation complex.

Nature structural & molecular biology·2026
Same author

NAC controls nascent chain fate through tunnel sensing and chaperone action.

Nature·2025
Same author

Selective silencing of antibiotic-tethered ribosomes as a resistance mechanism against aminoglycosides.

Nature communications·2025
Same author

Mechanisms and Determinants of -1 Ribosome Frameshifting and Bypassing.

Cold Spring Harbor perspectives in biology·2025
Same author

Cotranslational protein folding through non-native structural intermediates.

Science advances·2025
Same author

NAC controls nascent chain fate through tunnel sensing and chaperone action.

bioRxiv : the preprint server for biology·2025

Related Experiment Video

Updated: Apr 11, 2026

Live-Cell Imaging of Transcriptional Activity at DNA Double-Strand Breaks
09:07

Live-Cell Imaging of Transcriptional Activity at DNA Double-Strand Breaks

Published on: September 20, 2021

3.2K

Partitioning between recoding and termination at a stop codon-selenocysteine insertion sequence.

Suresh Babu Kotini1, Frank Peske1, Marina V Rodnina2

  • 1Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Goettingen, Germany.

Nucleic Acids Research
|June 5, 2015
PubMed
Summary

Selenocysteine (Sec) is incorporated into proteins by recoding UGA stop codons. This study reveals recoding efficiency is 30-40% and RF2 termination is less competitive than previously thought.

More Related Videos

Subcloning Plus Insertion SPI - A Novel Recombineering Method for the Rapid Construction of Gene Targeting Vectors
09:02

Subcloning Plus Insertion SPI - A Novel Recombineering Method for the Rapid Construction of Gene Targeting Vectors

Published on: January 8, 2015

17.2K
Gene-targeted Random Mutagenesis to Select Heterochromatin-destabilizing Proteasome Mutants in Fission Yeast
07:18

Gene-targeted Random Mutagenesis to Select Heterochromatin-destabilizing Proteasome Mutants in Fission Yeast

Published on: May 15, 2018

11.2K

Related Experiment Videos

Last Updated: Apr 11, 2026

Live-Cell Imaging of Transcriptional Activity at DNA Double-Strand Breaks
09:07

Live-Cell Imaging of Transcriptional Activity at DNA Double-Strand Breaks

Published on: September 20, 2021

3.2K
Subcloning Plus Insertion SPI - A Novel Recombineering Method for the Rapid Construction of Gene Targeting Vectors
09:02

Subcloning Plus Insertion SPI - A Novel Recombineering Method for the Rapid Construction of Gene Targeting Vectors

Published on: January 8, 2015

17.2K
Gene-targeted Random Mutagenesis to Select Heterochromatin-destabilizing Proteasome Mutants in Fission Yeast
07:18

Gene-targeted Random Mutagenesis to Select Heterochromatin-destabilizing Proteasome Mutants in Fission Yeast

Published on: May 15, 2018

11.2K

Area of Science:

  • Molecular Biology
  • Protein Synthesis
  • Biochemistry

Background:

  • Selenocysteine (Sec) insertion into proteins relies on recoding UGA stop codons.
  • This process is thought to be inefficient due to RF2-mediated termination.

Purpose of the Study:

  • To investigate the efficiency of UGA recoding for selenocysteine insertion.
  • To determine the role of RF2 in this process and understand the underlying mechanism.

Main Methods:

  • In vivo and in vitro experiments using mRNA fragments encoding selenoproteins.
  • Analysis of ribosome behavior at UGA codons and competition between Sec machinery and RF2.

Main Results:

  • In vivo recoding efficiency was 30-40%, independent of cell growth rate.
  • Efficient recoding requires adequate selenium levels; RF2 is a poor competitor.
  • In vitro studies confirmed limited Sec insertion capacity (40%) even without RF2.

Conclusions:

  • RF2 terminates translation only after failed Sec incorporation, not directly competing with the Sec machinery.
  • Early recruitment of Sec factors to the SECIS element prioritizes recoding over termination at Sec-specific UGA codons.