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Related Concept Videos

Chromatin Structure Regulates pre-mRNA Processing02:41

Chromatin Structure Regulates pre-mRNA Processing

In eukaryotic cells, nascent mRNA transcripts need to undergo many post-transcriptional modifications to reach the cell cytoplasm and translate into functional proteins. For a long time, transcription and pre-mRNA processing were considered two independent events that occur sequentially in the cell. However, it has now been well established that transcription and pre-mRNA processing are two simultaneous processes that are precisely regulated inside the cell.
The chromatin structure, especially...
Pre-mRNA Processing: Modification of pre-mRNA Ends01:35

Pre-mRNA Processing: Modification of pre-mRNA Ends

In eukaryotic cells, transcripts made by RNA polymerase are modified and processed before exiting the nucleus. Unprocessed RNA is called precursor mRNA or pre-mRNA to distinguish it from mature mRNA.
Once about 20-40 ribonucleotides have been joined together by RNA polymerase, a group of enzymes adds a cap to the 5' end of the growing transcript. In this process, a 5' phosphate is replaced by modified guanosine that has a methyl group attached (7-methyl guanosine). This 5' cap helps the cell...
pre-mRNA Processing02:01

pre-mRNA Processing

In eukaryotic cells, transcripts made by RNA polymerase are modified and processed before exiting the nucleus. Unprocessed RNA is called precursor mRNA or pre-mRNA to distinguish it from mature mRNA.
Once about 20-40 ribonucleotides have been joined together by RNA polymerase, a group of enzymes adds a “cap” to the 5’ end of the growing transcript. In this process, a 5’ phosphate is replaced by modified guanosine that has a methyl group attached to it (7-Methyl guanosine). This 5’ cap helps the...
Pre-mRNA Processing02:01

Pre-mRNA Processing

In eukaryotic cells, transcripts made by RNA polymerase are modified and processed before exiting the nucleus. Unprocessed RNA is called precursor mRNA or pre-mRNA to distinguish it from mature mRNA.
Once about 20-40 ribonucleotides have been joined together by RNA polymerase, a group of enzymes adds a “cap” to the 5’ end of the growing transcript. In this process, a 5’ phosphate is replaced by modified guanosine that has a methyl group attached to it (7-Methyl guanosine). This 5’ cap helps the...
Regulation of Expression at Multiple Steps01:23

Regulation of Expression at Multiple Steps

The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the addition of a...
Co-activators and Co-repressors02:04

Co-activators and Co-repressors

Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...

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Related Experiment Video

Updated: Jul 18, 2026

Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro
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Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro

Published on: May 3, 2014

Multiple histone deacetylases and the CREB-binding protein regulate pre-mRNA 3'-end processing.

Tadahiro Shimazu1, Sueharu Horinouchi2, Minoru Yoshida3

  • 1Chemical Genetics Laboratory, Discovery Research Institute, RIKEN, Wako, Saitama 351-0198, Japan; Department of Biotechnology, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan, and.

The Journal of Biological Chemistry
|December 19, 2006
PubMed
Summary

Trichostatin A (TSA) treatment acetylates cleavage factor Im subunit 25 (CFIm25) and poly(A) polymerase (PAP), impacting their interaction and PAP

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Single-step Purification of Macromolecular Complexes Using RNA Attached to Biotin and a Photo-cleavable Linker
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Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
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Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark

Published on: January 26, 2018

Related Experiment Videos

Last Updated: Jul 18, 2026

Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro
09:16

Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro

Published on: May 3, 2014

Single-step Purification of Macromolecular Complexes Using RNA Attached to Biotin and a Photo-cleavable Linker
08:12

Single-step Purification of Macromolecular Complexes Using RNA Attached to Biotin and a Photo-cleavable Linker

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Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
10:09

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark

Published on: January 26, 2018

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Post-translational Modifications

Background:

  • Histone deacetylase (HDAC) inhibitors like Trichostatin A (TSA) are known to induce protein acetylation.
  • Acetylation of non-histone proteins plays crucial roles in regulating various cellular processes.
  • The 3'-end processing of pre-mRNA involves complex protein interactions and modifications.

Purpose of the Study:

  • To identify non-histone proteins acetylated by Trichostatin A (TSA).
  • To investigate the functional consequences of TSA-induced acetylation on specific proteins involved in mRNA processing.
  • To elucidate the roles of specific histone deacetylases (HDACs) and acetyltransferases in regulating these modifications.

Main Methods:

  • Affinity purification using anti-acetylated lysine (AcLys) antibody.
  • Mass spectrometry for protein identification.
  • In vivo deacetylation assays with specific HDACs and sirtuins.
  • Analysis of protein-protein interactions and subcellular localization.

Main Results:

  • CFIm25 and PAP were identified as novel targets of TSA-induced acetylation.
  • Acetylation sites were mapped to interaction regions, affecting CFIm25-PAP complex formation.
  • CBP (CREB-binding protein) mediated acetylation, while HDAC1, HDAC3, HDAC10, SIRT1, and SIRT2 mediated deacetylation.
  • Acetylation of PAP inhibited its nuclear import by disrupting importin binding.

Conclusions:

  • CBP and HDACs regulate the 3'-end pre-mRNA processing machinery through acetylation/deacetylation.
  • Protein acetylation dynamically controls the interaction between PAP and the CFIm complex.
  • The acetylation status of PAP is critical for its proper nuclear localization and function.