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Related Concept Videos

RNA Editing02:23

RNA Editing

RNA editing is a post-transcriptional modification where a precursor mRNA (pre-mRNA) nucleotide sequence is changed by base insertion, deletion, or modification. The extent of RNA editing varies from a few hundred bases, in mitochondrial DNA of trypanosomes, to a just single base, in nuclear genes of mammals. Even a single base change in the pre-mRNA can convert a codon for one amino acid into the codon for another amino acid or a stop codon. This type of re-coding can significantly affect the...
Alternative RNA Splicing02:18

Alternative RNA Splicing

Alternative RNA splicing is the regulated splicing of exons and introns to produce different mature mRNAs from a single pre-mRNA. Unlike in constitutive splicing where a single gene produces a single type of mRNA, alternative splicing allows an organism to produce multiple proteins from a single gene and plays an important role in protein diversity.
There are five types of alternative RNA splicing that vary in the ways the pre-mRNA segments are removed or retained in the mature mRNA. The first...
Experimental RNAi02:15

Experimental RNAi

RNA interference (RNAi) is a cellular mechanism that inhibits gene expression by suppressing its transcription or activating the RNA degradation process. The mechanism was discovered by Andrew Fire and Craig Mello in 1998 in plants. Today, it is observed in almost all eukaryotes, including protozoa, flies, nematodes, insects, parasites, and mammals. This precise cellular mechanism of gene silencing has been developed into a technique that provides an efficient way to identify and determine the...
RNA Splicing01:32

RNA Splicing

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...
Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

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,...
Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...

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A Nonsequencing Approach for the Rapid Detection of RNA Editing
08:50

A Nonsequencing Approach for the Rapid Detection of RNA Editing

Published on: April 21, 2022

Evidence for insertional RNA editing in humans.

Alexandre Zougman1, Piotr Ziółkowski, Matthias Mann

  • 1Department of Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.

Current Biology : CB
|November 11, 2008
PubMed
Summary

Scientists discovered a new human RNA editing mechanism. This process creates altered protein forms by translating 5' untranslated regions, leading to N-terminally extended proteins.

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CRISPR/Cas9 Editing of the C. elegans rbm-3.2 Gene using the dpy-10 Co-CRISPR Screening Marker and Assembled Ribonucleoprotein Complexes.
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CRISPR/Cas9 Editing of the C. elegans rbm-3.2 Gene using the dpy-10 Co-CRISPR Screening Marker and Assembled Ribonucleoprotein Complexes.

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A Nonsequencing Approach for the Rapid Detection of RNA Editing
08:50

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Published on: April 21, 2022

CRISPR/Cas9 Editing of the C. elegans rbm-3.2 Gene using the dpy-10 Co-CRISPR Screening Marker and Assembled Ribonucleoprotein Complexes.
07:46

CRISPR/Cas9 Editing of the C. elegans rbm-3.2 Gene using the dpy-10 Co-CRISPR Screening Marker and Assembled Ribonucleoprotein Complexes.

Published on: December 11, 2020

Area of Science:

  • Molecular Biology
  • Proteomics
  • Genetics

Background:

  • Mass spectrometry (MS)-based proteomics offers insights beyond gene-level analysis.
  • Unassigned peptide information in proteomics experiments can reveal novel biological mechanisms.
  • Linker histones H1 and high-mobility group (HMG) proteins are key regulators of gene expression via chromatin structure.

Purpose of the Study:

  • To investigate unassigned peptide information from large-scale proteomics experiments.
  • To discover novel mechanisms of protein alteration.
  • To characterize the function of N-terminally extended (ET) proteins.

Main Methods:

  • High-resolution mass spectrometry (MS) analysis of histone H1 and HMG protein fractions from human cells.
  • Bioinformatic analysis of Expressed Sequence Tag (EST) databases.
  • Investigation of RNA editing mechanisms.

Main Results:

  • Discovered peptides mapping upstream of known translation start sites for H1 and HMG proteins.
  • Identified N-terminally extended (ET) proteins resulting from in-frame translation of 5' untranslated regions (5'UTR).
  • Revealed a novel RNA editing mechanism involving a single uridine insertion creating new translation start sites.

Conclusions:

  • This study reports the first instance of RNA-insertion editing in humans.
  • The findings highlight the potential of proteomics to uncover previously unknown biological processes.
  • This mechanism explains the generation of N-terminally extended H1 and HMG proteins.