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Origin of octameric creatine kinases

W R Ellington1, K Roux, A O Pineda

  • 1Department of Biological Science and Institute of Molecular Biophysics, Florida State University, Tallahassee 32306-4370, USA. elling@bio.fsu.edu

FEBS Letters
|April 16, 1998
PubMed
Summary

Octameric mitochondrial creatine kinase (MiCK) is found in protostomes, not just deuterostomes. This ancient octamerization predates the split between protostome and deuterostome lineages.

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Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Molecular Biology

Background:

  • Mitochondrial creatine kinase (MiCK) is typically octameric in vertebrates and echinoderms.
  • This octameric structure is believed to be crucial for function and mitochondrial localization.

Purpose of the Study:

  • To investigate the quaternary structure of creatine kinase (CK) in the polychaete Chaetopterus variopedatus spermatozoa.
  • To determine if octameric CK is exclusive to deuterostomes or has an earlier evolutionary origin.

Main Methods:

  • Isolation and characterization of three creatine kinase isoenzymes (CK1, CK2, CK3) from C. variopedatus sperm.
  • Gel permeation chromatography (Superdex 200HR) to determine native molecular mass.
  • Electron microscopy of negatively stained CK3 preparations.

Main Results:

  • CK3, found in the sperm head/midpiece, has a subunit molecular mass of 43.4 kDa.
  • Gel permeation chromatography indicated a native molecular mass of 344.9 kDa for CK3, consistent with an octamer.
  • Electron micrographs of CK3 were structurally similar to vertebrate octameric MiCK.

Conclusions:

  • CK3 from C. variopedatus shares significant similarities with MiCKs from vertebrates and echinoderms.
  • Octamerization of creatine kinase is an ancient trait, predating the divergence of protostomes and deuterostomes.
  • The presence of octameric CK in a protostome challenges the notion of it being an advanced feature exclusive to deuterostomes.

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