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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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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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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
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Intrinsically Disordered Regions Define Unique Protein Interaction Networks in CHD Family Remodelers.

Mehdi Sharifi Tabar1,2,3, Chirag Parsania1,2,3, Caroline Giardina2

  • 1Faculty of Medicine & Health, The University of Sydney, Camperdown, New South Wales, Australia.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|May 15, 2025
PubMed
Summary

Chromodomain helicase DNA-binding (CHD) enzymes

Keywords:
DNA helicaseaggregation‐prone regionschromatin remodelersintrinsically disordered regionsprotein–protein interactionstranscription

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Chromodomain helicase DNA-binding (CHD) enzymes are crucial for genome regulation.
  • Their N- and C-termini are intrinsically disordered and poorly understood.
  • These termini are vital for protein-protein interactions and complex formation.

Purpose of the Study:

  • To identify novel protein-protein interactions (PPIs) in the N- and C-termini of human CHD proteins.
  • To characterize the function of a conserved aggregation-prone region (APR) in CHD4.
  • To investigate the role of CHD4 APR in transcriptional regulation.

Main Methods:

  • Mass spectrometry was employed to identify protein-protein interactions.
  • Biochemical assays were used to define the role of the CHD4 APR.
  • Gene transcription analysis was performed during erythrocyte formation.

Main Results:

  • Dozens of novel PPIs involving CHD N- and C-termini were identified.
  • A conserved aggregation-prone region (APR) in CHD4 was defined and shown to be critical for NuRD and ChAHP complex interactions.
  • The CHD4 APR regulates gene transcription in erythrocyte development.

Conclusions:

  • The intrinsically disordered N- and C-termini of CHD proteins mediate critical protein interactions.
  • The CHD4 APR is a key regulatory element in chromatin remodeling complexes.
  • These interactions shape unique transcriptional programs essential for cellular functions like erythrocyte formation.