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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Conservation of Protein Domains Over Different Proteins02:26

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
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MRG Proteins Are Shared by Multiple Protein Complexes With Distinct Functions.

Maëva Devoucoux1, Céline Roques1, Catherine Lachance1

  • 1St. Patrick Research Group in Basic Oncology, Laval University Cancer Research Center, Oncology Division of CHU de Québec-Université Laval Research Center, Quebec City, Quebec, Canada.

Molecular & Cellular Proteomics : MCP
|May 31, 2022
PubMed
Summary
This summary is machine-generated.

MRG15 and MRGX proteins associate with key chromatin regulators and DNA repair complexes. A novel human TINTIN complex involving MRG15/X, MRGBP, BRD8, and EP400NL plays a role in gene transcription.

Keywords:
MRG domainchromodomainhistone acetylationhistone methylationtranscription

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chromatin Biology

Background:

  • MRG15/MORF4L1 is a conserved eukaryotic protein with a chromodomain (CHD) that binds histone H3 lysine 36 trimethylation (H3K36me3).
  • MRG15 is known to interact with factors involved in chromatin modification, gene regulation, mRNA splicing, and DNA repair.
  • A comprehensive understanding of MRG15's native interactome under physiological conditions is lacking.

Purpose of the Study:

  • To identify and characterize the stable native protein complexes associated with human MRG15, MRGX/MORF4L2, and MRGBP.
  • To investigate the functional significance of these protein associations in chromatin-based nuclear processes.
  • To elucidate the composition and function of a newly identified MRG15/X-MRGBP-BRD8-EP400NL complex.

Main Methods:

  • Genome editing and tandem affinity purification were used to analyze the native interactome of MRG15, MRGX, and MRGBP in K562 cells.
  • CRISPR tagging of endogenous proteins and isoform comparison were employed for confirmation.
  • Point mutations were introduced based on structural information to disrupt specific complex associations.

Main Results:

  • MRG15 and MRGX showed stable, interchangeable associations with NuA4/TIP60, Sin3B, ASH1L, and PALB2-BRCA2 complexes.
  • A novel, abundant native complex, MRG15/X-MRGBP-BRD8-EP400NL, was identified, functionally resembling the yeast TINTIN complex.
  • EP400NL competes for BRD8 binding, forming TINTIN, which is implicated in the transcription of specific genes via BRD8's H4ac-binding and MRG15's H3K36me3-binding domains.

Conclusions:

  • The study provides a detailed map of human MRG protein-associated complexes, revealing their dynamic interactions.
  • The newly discovered human TINTIN complex plays a role in gene transcription, integrating epigenetic marks.
  • These findings enhance the understanding of MRG proteins' diverse functions in chromatin regulation and nuclear processes.