Functional evidence for in vitro microtubule severing by the plant katanin homologue

Biochem J. 2002 Jul 15;365(Pt 2):337-42. doi: 10.1042/BJ20020689.


Temporal and spatial assembly of microtubules in plant cells depends mainly on the activity of microtubule-interacting proteins, which either stabilize, destabilize or translocate microtubules. Recent data have revealed that the thale cress (Arabidopsis thaliana) contains a protein related to the p60 catalytic subunit of animal katanin, a microtubule-severing protein. However, effects of the plant p60 on microtubule assembly are not known. We report the first functional evidence that the recombinant A. thaliana p60 katanin subunit, Atp60, binds to microtubules and severs them in an ATP-dependent manner in vitro. ATPase activity of Atp60 is stimulated by low tubulin/katanin ratios, and is inhibited at higher ratios. Considering its properties in vitro, several functions of Atp60 in vivo are discussed.

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / isolation & purification
  • Adenosine Triphosphatases / metabolism*
  • Arabidopsis / metabolism*
  • Base Sequence
  • Cloning, Molecular
  • DNA Primers
  • Katanin
  • Microtubules / metabolism*
  • Molecular Sequence Data
  • Protein Binding
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism


  • DNA Primers
  • Recombinant Proteins
  • Adenosine Triphosphatases
  • Katanin

Associated data

  • GENBANK/AF048706
  • GENBANK/AF358779