Proteolysis of tubulin isotypes within Tetrahymena axonemes

Biol Chem Hoppe Seyler. 1995 Dec;376(12):729-32. doi: 10.1515/bchm3.1995.376.12.729.


In the axonemes of Tetrahymena cilia, beta-tubulin was digested more rapidly by chymotrypsin than alpha-tubulin. On the other hand, in the solubilized state, both tubulins were digested by the protease at almost the same rate. Among alpha-tubulin isotypes within the axonemes, alpha 5-tubulin was more rapidly digested by chymotrypsin than other alpha-tubulin isotypes. The addition of ATP and vanadate (Vi) to the axonemes significantly protected the alpha 5-isotype from chymotryptic proteolysis. These tendencies could not be observed in tubulins solubilized from axonemes. Based on the case of the alpha 5-tubulin isotype, it is possible to negate the idea that all tubulin isotypes are distributed homogeneously and play similar functional roles within the axonemes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / chemistry
  • Animals
  • Chymotrypsin
  • Electrophoresis, Polyacrylamide Gel
  • Hydrolysis
  • Isoelectric Focusing
  • Isomerism
  • Microtubules / metabolism*
  • Tetrahymena pyriformis / metabolism*
  • Tubulin / metabolism*
  • Vanadates / chemistry


  • Tubulin
  • Vanadates
  • Adenosine Triphosphate
  • Chymotrypsin