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

Initiation of Translation02:33

Initiation of Translation

40.6K
Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
40.6K
Initiation of Translation02:33

Initiation of Translation

8.7K
8.7K
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
Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

15.3K
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,...
15.3K
Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

4.9K
4.9K
Improving Translational Accuracy02:07

Improving Translational Accuracy

15.7K
Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
15.7K

You might also read

Related Articles

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

Sort by
Same author

Structural basis for non-AUG translation regulation by 5MPs.

bioRxiv : the preprint server for biology·2026
Same author

Author Correction: Cryo-EM structure of a natural RNA nanocage.

Nature·2025
Same author

Structural mechanism of mRNA decoding by mammalian GTPase GTPBP1.

Nature communications·2025
Same author

Structural mechanism of mRNA decoding by mammalian GTPase GTPBP1.

bioRxiv : the preprint server for biology·2025
Same author

Translon: a single term for translated regions.

Nature methods·2025
Same author

Cryo-EM structure of a natural RNA nanocage.

Nature·2025

Related Experiment Video

Updated: Apr 15, 2026

Dual DNA Rulers to Study the Mechanism of Ribosome Translocation with Single-Nucleotide Resolution
10:27

Dual DNA Rulers to Study the Mechanism of Ribosome Translocation with Single-Nucleotide Resolution

Published on: July 8, 2019

6.7K

A Unified Mechanism of +1 Ribosomal Frameshifting.

Ivan Sorokin1, Andrei A Korostelev2

  • 1Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen 9747 AG, Netherlands.

Cold Spring Harbor Perspectives in Biology
|April 13, 2026
PubMed
Summary

Ribosomes normally maintain the mRNA frame, but frameshifting allows making multiple proteins from one mRNA. This review explores +1 frameshifting (+1FS) mechanisms, including tRNA modifications and quadruplet decoding.

More Related Videos

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis
08:07

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis

Published on: July 6, 2021

3.2K
Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation
12:26

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

Published on: February 12, 2022

6.1K

Related Experiment Videos

Last Updated: Apr 15, 2026

Dual DNA Rulers to Study the Mechanism of Ribosome Translocation with Single-Nucleotide Resolution
10:27

Dual DNA Rulers to Study the Mechanism of Ribosome Translocation with Single-Nucleotide Resolution

Published on: July 8, 2019

6.7K
Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis
08:07

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis

Published on: July 6, 2021

3.2K
Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation
12:26

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

Published on: February 12, 2022

6.1K

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Ribosomes translate messenger RNA (mRNA) in discrete 3-nucleotide codon steps.
  • Frameshifting, a deviation from standard translation, expands protein diversity from a single mRNA.
  • Understanding frameshifting regulation is crucial for cellular and viral processes.

Purpose of the Study:

  • To review recent advancements in understanding +1 frameshifting (+1FS).
  • To explore mechanisms inducing and regulating +1FS.
  • To propose a unifying structural model for +1FS.

Main Methods:

  • Structural and biochemical studies of +1FS.
  • Analysis of mRNA slippery sequences and transfer RNA (tRNA) structures.
  • Exploration of quadruplet decoding using modified tRNAs.

Main Results:

  • Insights into +1FS induced by specific mRNA sequences and tRNA stem-loop structures.
  • Evaluation of quadruplet decoding as a tool for genetic code expansion.
  • Discussion of +1FS in bacterial and eukaryotic systems.

Conclusions:

  • A unifying structural mechanism for +1FS is proposed.
  • +1FS plays a significant role in expanding coding capacity.
  • Further research into frameshifting mechanisms can yield biotechnological applications.