Proteolysis of tubulin isotypes within Tetrahymena axonemes.
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.
Nakamura
K
K
Department of Health Science, Hiroshima Women's University, Japan.
Shigaki
Y
Y
Takaya
C
C
D000255:Adenosine Triphosphate / Q000737:chemistry; D000818:Animals; D002918:Chymotrypsin; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D007525:Isoelectric Focusing; D007536:Isomerism; D008870:Microtubules / Q000378:metabolism*; D013769:Tetrahymena pyriformis / Q000378:metabolism*; D014404:Tubulin / Q000378:metabolism*; D014638:Vanadates / Q000737:chemistry
D014404:Tubulin; D014638:Vanadates; D000255:Adenosine Triphosphate; D002918:Chymotrypsin