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A context-dependent and disordered ubiquitin-binding motif.

Jesper E Dreier1,2, Andreas Prestel1, João M Martins3

  • 1Structural Biology and NMR Laboratory, University of Copenhagen, Ole Maaloes Vej 5, 2200, Copenhagen N, Denmark.

Cellular and Molecular Life Sciences : CMLS
|August 16, 2022
PubMed
Summary
This summary is machine-generated.

Researchers discovered a new Disordered Ubiquitin-Binding Motif (DisUBM) that binds ubiquitin without folding. This motif expands the known ways proteins recognize ubiquitylation, impacting degradation and transcription processes.

Keywords:
ContextCyclic peptideDeep mutational scanningIDPNMRSLiMUBMUbiquitin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Ubiquitin conjugation is a key posttranslational modification.
  • Folded protein domains typically recognize ubiquitin.
  • Previous studies suggested protein regions might fold upon binding ubiquitin.

Purpose of the Study:

  • To identify and characterize novel ubiquitin-binding motifs.
  • To expand the known repertoire of ubiquitin-binding proteins.
  • To understand the biophysical basis of disordered ubiquitin recognition.

Main Methods:

  • Peptide binding arrays
  • Bioinformatics analysis
  • NMR spectroscopy
  • De novo peptide library screening

Main Results:

  • A novel Disordered Ubiquitin-Binding Motif (DisUBM) was identified.
  • DisUBMs remain disordered upon ubiquitin binding.
  • The motif's binding relies on aromatic and charged residues, not fixed positions.
  • Binding affinity is low but enhanced by the surrounding disordered protein chain.
  • DisUBMs are found in proteins involved in degradation and transcription.

Conclusions:

  • DisUBMs represent a new class of ubiquitin-binding elements.
  • These motifs expand the mechanisms for translating ubiquitylation signals.
  • Disordered ubiquitin-binding motifs can function as affinity enhancers in intrinsically disordered proteins.