Jove
Visualize
Contact Us

Related Concept Videos

Stringent Response in E. coli01:23

Stringent Response in E. coli

469
Bacterial growth is closely tied to nutrient availability, with cells proliferating exponentially under favorable conditions and entering a stationary phase when resources become scarce. This transition is mediated by a regulatory mechanism known as the stringent response, which allows bacteria to adapt to nutrient deprivation by modulating gene expression and metabolic activity.During nutrient scarcity, intracellular amino acid levels decline. It results in the accumulation of uncharged tRNAs...
469
Termination of Translation01:44

Termination of Translation

28.8K
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...
28.8K
Termination of Translation01:44

Termination of Translation

7.1K
7.1K
Improving Translational Accuracy02:07

Improving Translational Accuracy

15.5K
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...
15.5K
Initiation of Translation02:33

Initiation of Translation

40.3K
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...
40.3K
Initiation of Translation02:33

Initiation of Translation

8.6K
8.6K

You might also read

Related Articles

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

Sort by
Same author

Corrigendum to: "The endonuclease MCPIP1 protects against liver cancer development in a sex-dependent manner by modulating β-catenin and CREB1" [JHEP Reports 8 (2026) 101755].

JHEP reports : innovation in hepatology·2026
Same author

Conserved and Divergent Modes of Substrate Interaction Define Selective Localizations and Functions of a Cdc14 Phosphatase.

Molecular biology of the cell·2026
Same author

EasyGrid: a versatile platform for automated cryo-EM sample preparation and quality control.

Nature methods·2026
Same author

Alternative ribosomal protein RpmE2 is produced under zinc limitation in <i>Neisseria gonorrhoeae</i> and slows translation and bacterial growth.

mBio·2026
Same author

SNOR promotes translation restart after dormancy.

Nature·2026
Same author

The endonuclease MCPIP1 protects against liver cancer development in a sex-dependent manner by modulating β-catenin and CREB1.

JHEP reports : innovation in hepatology·2026
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 Experiment Video

Updated: Apr 4, 2026

Analysis of Translation Initiation During Stress Conditions by Polysome Profiling
10:59

Analysis of Translation Initiation During Stress Conditions by Polysome Profiling

Published on: May 19, 2014

18.9K

A Novel Eukaryotic Ribosome Factor Enables Translation Restart Following Cellular Dormancy.

Maciej Gluc1,2, Higor Rosa3,4,2, Maria Bozko1

  • 1Department of Molecular Physiology and Biological Physics and Center for Cell and Membrane Physiology, University of Virginia, Charlottesville, VA 22903, USA.

Biorxiv : the Preprint Server for Biology
|April 3, 2026
PubMed
Summary

Scientists discovered SNOR, a protein that halts protein synthesis during cellular dormancy caused by glucose depletion. This factor is crucial for restarting protein production when nutrients return, revealing a new mechanism for stress response in fungi.

More Related Videos

Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells
14:29

Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells

Published on: December 25, 2021

4.9K
Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs
10:37

Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs

Published on: May 10, 2018

13.3K

Related Experiment Videos

Last Updated: Apr 4, 2026

Analysis of Translation Initiation During Stress Conditions by Polysome Profiling
10:59

Analysis of Translation Initiation During Stress Conditions by Polysome Profiling

Published on: May 19, 2014

18.9K
Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells
14:29

Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells

Published on: December 25, 2021

4.9K
Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs
10:37

Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs

Published on: May 10, 2018

13.3K

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Structural Biology

Background:

  • Dormancy is a survival strategy across all life domains, involving global protein synthesis shutdown to endure stress.
  • Molecular mechanisms of ribosome inactivation and reactivation during eukaryotic dormancy are not fully understood.

Purpose of the Study:

  • To identify molecular factors regulating ribosome function during induced dormancy in eukaryotes.
  • To elucidate the role of novel ribosome-associated factors in stress response and protein synthesis regulation.

Main Methods:

  • Identification of SNOR (SBDS-like ribosome-associated factor) in Schizosaccharomyces pombe.
  • Analysis of SNOR association with ribosomes during glucose-depletion-induced dormancy.
  • In situ structural biology to probe SNOR's interaction with the ribosome.

Main Results:

  • SNOR is upregulated and binds to ribosomes during glucose starvation, inhibiting protein synthesis.
  • SNOR interacts with the peptidyl transferase center (PTC), blocks tRNA binding, and caps the polypeptide exit tunnel (PET).
  • SNOR is essential for resuming protein synthesis upon glucose reintroduction and exiting dormancy.

Conclusions:

  • SNOR is a novel ribosome-associated factor linking glucose stress, dormancy, and protein synthesis surveillance.
  • SNOR plays a critical role in both repressing and restarting protein synthesis during cellular stress.
  • The findings highlight SNOR's evolutionary conservation in fungi and its importance in stress-responsive translation regulation.