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Fuzzy Interactions Form and Shape the Histone Transport Complex.

Nives Ivic1, Mia Potocnjak2, Victor Solis-Mezarino2

  • 1Gene Center Munich and Department of Biochemistry, Ludwig Maximilian University of Munich, 81377 Munich, Germany; Department of Physical Chemistry, Rudjer Boskovic Institute, 10000 Zagreb, Croatia.

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Summary

Two importins form a cradle to transport histone H1 into the nucleus. Specific motifs in importin 7 (Imp7) are crucial for this process and complex disassembly.

Keywords:
IDPImp7Impβcryo-EMdisordered proteinshistone H1karyopherinsnuclear importtransport receptors

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Nuclear import of proteins is essential for cellular function.
  • Highly charged proteins, like histone H1 and ribosomal proteins, require a dimer of transport receptors for import.
  • Understanding the structural basis of these import processes is key to cellular regulation.

Purpose of the Study:

  • To determine the cryo-electron microscopy (cryo-EM) structure of the importin 7 (Imp7):importin β (Impβ):histone H1.0 (H1.0) complex.
  • To elucidate the mechanism by which importins facilitate the nuclear import of charged proteins.
  • To identify key structural features and motifs involved in complex formation and disassembly.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine the high-resolution structure of the Imp7:Impβ:H1.0 complex.
  • Structural analysis to understand the interactions between importins and histone H1.
  • Biochemical assays to investigate the role of specific motifs (GGxxF, FxFG) in Imp7.

Main Results:

  • The structure reveals that two importins form a cradle-like structure accommodating histone H1.
  • The globular domain of H1.0 binds to Impβ, while its C-terminal tail is chaperoned by acidic loops of Impβ and Imp7.
  • The disordered H1 tail acts as a zipper, stabilizing the complex via transient interactions.
  • GGxxF and FxFG motifs in Imp7 are essential for Imp7:Impβ dimerization and H1 import, promoting complex disassembly.

Conclusions:

  • The Imp7:Impβ dimer forms a unique cradle for the nuclear import of histone H1.
  • Disordered regions and transient electrostatic interactions play a significant role in stabilizing protein complexes.
  • The identified motifs in Imp7 are critical for importin dimerization and subsequent complex disassembly, similar to interactions with nucleoporins.