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Ferritin Assembly Revisited: A Time-Resolved Small-Angle X-ray Scattering Study.

Daisuke Sato1, Hideaki Ohtomo1, Yoshiteru Yamada2

  • 1Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577, Japan.

Biochemistry
|December 23, 2015
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Summary

Escherichia coli ferritin A (EcFtnA) reassembles from dimers into a 24-subunit cage after a pH increase. Time-resolved SAXS revealed intermediate oligomers, suggesting a complex assembly pathway.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Escherichia coli ferritin A (EcFtnA) forms a 24-subunit cage-like structure.
  • This structure dissociates into dimers at acidic pH.
  • EcFtnA dimers retain native structure and can reassemble upon pH increase.

Purpose of the Study:

  • To investigate the reassembly mechanism of EcFtnA from dimers to a 24-mer.
  • To identify intermediate species during the EcFtnA assembly reaction.
  • To determine the kinetics and reaction order of EcFtnA reassembly.

Main Methods:

  • Time-resolved small-angle X-ray scattering (TR-SAXS) was employed to monitor the reassembly process in real-time.
  • Protein concentration dependence was analyzed to determine reaction orders.
  • SAXS profiles were analyzed to model intermediate oligomer formation.

Main Results:

  • TR-SAXS data indicated the presence of intermediate oligomers during EcFtnA reassembly.
  • The initial reassembly reaction kinetics were a mixture of second- and third-order processes, suggesting tetramer and hexamer formation.
  • A simplified model considering tetramers, hexamers, and dodecamers as intermediates could explain the observed SAXS profile changes.

Conclusions:

  • The reassembly of EcFtnA is a multi-step process involving transient intermediate oligomers.
  • The initial steps involve the formation of tetrameric and hexameric species.
  • TR-SAXS is a powerful tool for elucidating the dynamic assembly pathways of protein complexes.