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Dynamics and structural features of the eEF1A1 and eEF1A2 paralogs.

Oleksandra Novosylna1, Vyacheslav Shalak1, Katarzyna Dąbrowska2

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Translation factors eEF1A1 and eEF1A2, despite high similarity, show distinct dynamics and structures. These differences explain their varied roles in human diseases and protein interactions.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Translation elongation factors eEF1A1 and eEF1A2 share 97% sequence identity but have distinct expression patterns and disease associations.
  • The molecular basis for these paralog-specific differences, despite high homology, remains poorly understood.

Purpose of the Study:

  • To investigate the structural dynamics and conformational differences between eEF1A1 and eEF1A2.
  • To elucidate the molecular mechanisms underlying their distinct protein interactions and disease associations.

Main Methods:

  • Hydrogen-deuterium exchange mass spectrometry (HDX-MS)
  • Molecular dynamics (MD) simulations
  • Small-angle X-ray scattering (SAXS)

Main Results:

  • eEF1A1 and eEF1A2 exhibit distinct structural dynamics and organizations.
  • eEF1A2 is compact and stable, while eEF1A1 displays multiple conformations, including domain dynamics and dimerization.
  • eEF1A1 facilitates protein dimerization, unlike eEF1A2, challenging prior crystallographic data.

Conclusions:

  • Distinct structural dynamics explain functional divergence between eEF1A1 and eEF1A2.
  • These findings offer insights into paralog-specific non-translational roles and disease contributions.
  • The study reveals eEF1A1's propensity for dimerization, contrasting with eEF1A2's monomeric state.