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In vitro dimerization of human RIO2 kinase.

Frédérique Maurice1, Natacha Pérébaskine1, Stéphane Thore1

  • 1INSERM U1212, UMR CNRS 5320, Université de Bordeaux , Bordeaux , France.

RNA Biology
|August 9, 2019
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Summary
This summary is machine-generated.

Human RIO2 kinase forms a homodimer in vitro, unlike its fungal and archaeal counterparts. This dimerization remodels the ATP-binding pocket, suggesting a novel regulatory mechanism for this essential protein kinase.

Keywords:
40SRIO2Ribosome biogenesisatypical kinasedimerprotomer

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • RIO proteins are atypical protein kinases.
  • RIO2 (Ribosome Interacting Only 2) is a serine/threonine protein kinase/ATPase crucial for pre-40S ribosomal subunit maturation.
  • Previous structural studies of archaeal and fungal Rio2 proteins indicated a monomeric form.

Purpose of the Study:

  • To determine the atomic structures of human RIO2 kinase.
  • To investigate the oligomeric state and structural features of human RIO2.
  • To elucidate the mechanism of RIO2 kinase activity regulation through its oligomeric state.

Main Methods:

  • X-ray crystallography to obtain three atomic structures of human RIO2.
  • Biochemical analysis to study protein-protein interactions and enzyme activity.
  • Structural comparison with known archaeal and fungal Rio2 structures.

Main Results:

  • Human RIO2 kinase forms a homodimer in vitro.
  • Dimerization leads to partial remodeling of the ATP-binding pocket in each protomer, rendering it apostate (inactive).
  • Key residues involved in ATP binding and catalysis mediate homodimerization.

Conclusions:

  • Human RIO2 kinase exhibits an unusual homodimeric structure in vitro, distinct from its homologs.
  • This homodimerization mechanism, involving residues critical for catalysis, suggests a novel regulatory pathway.
  • The dimeric state may maintain RIO2 in an inactive conformation, potentially regulating its function in ribosome biogenesis or during protein import.