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

Improving Translational Accuracy02:07

Improving Translational Accuracy

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

Ribosomal RNA Synthesis

15.0K
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,...
15.0K
Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

4.7K
4.7K
Nonsense-mediated mRNA Decay02:27

Nonsense-mediated mRNA Decay

12.0K
The Upf proteins that carry out nonsense-mediated decay (NMD) are found in all eukaryotic organisms, including humans. Each protein has an individual role, but they need to work in collaboration. Upf1 is an ATP-dependent RNA helicase that unwinds the RNA helix. Because Upf1 can unwind any RNA, Upf2 and Upf3 are required to help Upf1 discriminate between nonsense and normal mRNAs.
Usually, Upf3 binds to an Exon Junction Complex (EJC) at mRNA splice sites. If a ribosome fully translates the mRNA,...
12.0K
Nonsense-mediated mRNA Decay02:27

Nonsense-mediated mRNA Decay

3.5K
3.5K
Leaky Scanning02:28

Leaky Scanning

5.8K
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...
5.8K

You might also read

Related Articles

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

Sort by
Same author

Structural basis of the regulation by CDK11 kinase of early spliceosome activation and evidence for its proofreading by DHX15 helicase.

Nature communications·2026
Same author

Membrane insertion of mitochondrial-encoded proteins regulates ribosome decoding speed.

Nature structural & molecular biology·2026
Same author

2'-O-methylation-dependent installation of N<sup>2</sup>-methylguanosine in the U6 internal stem loop facilitates efficient spliceosome assembly.

Nature communications·2026
Same author

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

Nature structural & molecular biology·2026
Same author

Controlled route to active turbulence: filling an activity spot with topological defects.

Soft matter·2026
Same author

The dual G9a inhibitor and histamine H3 receptor antagonist A-366 improves repetitive and social behaviors and attenuates neuroinflammation in BTBR T + tf/J mice.

Scientific reports·2026

Related Experiment Video

Updated: Mar 8, 2026

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

Ribosome dynamics during decoding.

Marina V Rodnina1, Niels Fischer2, Cristina Maracci3

  • 1Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen 37077, Germany rodnina@mpibpc.mpg.de.

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|February 1, 2017
PubMed
Summary
This summary is machine-generated.

Elongation factors EF-Tu and SelB deliver aminoacyl-tRNAs to the ribosome. Ribosome dynamics ensures high selectivity for correct aminoacyl-tRNA selection, maintaining translation speed and fidelity.

Keywords:
decodingrecodingribosometRNAtranslation

More Related Videos

De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data
08:23

De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data

Published on: February 18, 2022

4.2K
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

6.0K

Related Experiment Videos

Last Updated: Mar 8, 2026

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
De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data
08:23

De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data

Published on: February 18, 2022

4.2K
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

6.0K

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Elongation factors EF-Tu and SelB are GTPases essential for delivering aminoacyl-tRNAs (aa-tRNAs) to the ribosome during protein synthesis.
  • While EF-Tu facilitates canonical amino acid incorporation, SelB specifically decodes UGA codons for selenocysteine insertion.
  • The precise selection and delivery of aa-tRNAs involve intricate interactions with the ribosome.

Purpose of the Study:

  • To review recent advancements in understanding the role of ribosome dynamics in the selection of aa-tRNAs.
  • To elucidate the mechanisms by which canonical aa-tRNAs and selenocysteine-tRNA (tRNASec) achieve correct codon recognition.
  • To explore the GTPase activity of EF-Tu and SelB and the subsequent accommodation of aa-tRNA within the ribosome.

Main Methods:

  • This review synthesizes current research on ribosome dynamics and aa-tRNA selection.
  • It analyzes the conformational changes within the ribosome in response to correct and incorrect aa-tRNA binding.
  • Mechanisms of GTPase activation, GTP hydrolysis, and aa-tRNA accommodation are discussed.

Main Results:

  • Ribosome dynamics play a critical role in distinguishing cognate aa-tRNAs from non-cognate ones.
  • Both local and global ribosomal rearrangements are induced by correct and incorrect aa-tRNA binding.
  • The process involves GTPase activation and hydrolysis by EF-Tu and SelB, followed by aa-tRNA accommodation.

Conclusions:

  • Ribosome dynamics are crucial for ensuring high fidelity in aminoacyl-tRNA selection.
  • Conformational fluctuations, induced fit, and kinetic discrimination are key mechanisms that maintain translation speed and accuracy.
  • Understanding these dynamics provides insights into the fundamental processes of protein synthesis.