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Related Concept Videos

Ribosome Profiling02:24

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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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...
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Related Experiment Video

Updated: Jan 13, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
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Locus-specific quantification reveals dynamics of ribosomal ac4C modifications.

Ningning Qin1, Yin Wang1, Qiaoling Yuan1

  • 1College of Life Sciences & Hebei Basic Science Center for Biotic Interactions, Hebei University, Baoding, Hebei 071002, China.

New Biotechnology
|January 8, 2026
PubMed
Summary

Ribosomal N4-acetylcytidine (ac4C) modifications are dynamic epitranscriptomic marks that change with growth and stress. Their accumulation during rRNA maturation and interplay with other modifications are revealed using novel methods.

Keywords:
DynamicN4-acetylcytidine (ac4C)QuantificationrRNA maturation

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Single Nucleotide Polymorphism-sensitive FISH Detection of Locus-specific Ribosomal RNA Transcription in Drosophila melanogaster
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Area of Science:

  • Molecular Biology
  • Epitranscriptomics
  • Ribosome biogenesis

Background:

  • Eukaryotic ribosomes possess two conserved N4-acetylcytidine (ac4C) modifications in key functional areas.
  • Fundamental questions persist regarding ac4C deposition kinetics, dynamics, and interactions with other rRNA modifications.

Purpose of the Study:

  • To quantitatively profile ribosomal ac4C modifications during rRNA maturation and under varying conditions in Saccharomyces cerevisiae.
  • To investigate the dynamic nature and site-specific responses of ac4C modifications to growth phase and thermal stress.
  • To explore the interplay between ac4C modifications and other rRNA modifications, such as 2'-O-methylation.

Main Methods:

  • Quantitative profiling of ribosomal ac4C modifications using ac4C-Sanger sequencing.
  • Analysis of ac4C dynamics across rRNA precursors and mature rRNA under different conditions.
  • Orthogonal detection and quantification methods including High-Resolution Melting (HRM) and SELECT (single-base elongation- and ligation-based qPCR amplification).

Main Results:

  • ac4C accumulates progressively during 18S rRNA maturation with distinct kinetics for each site.
  • Ribosomal ac4C levels exhibit dynamic, site-specific responses to growth phase and thermal stress.
  • Genetic perturbation of snR40 impacts both ac4C sites differentially, suggesting complex regulatory interdependencies.

Conclusions:

  • Ribosomal ac4C is a dynamic epitranscriptomic mark influenced by rRNA maturation and cellular conditions.
  • The biogenesis of ac4C involves intricate interdependencies with other rRNA modifications.
  • Novel tools like ac4C-Sanger, HRM, and SELECT provide accessible methods for investigating ribosomal ac4C.