Effect of specific proteolytic cleavages on tubulin polymer formation.
The capacity for self-polymerization and shape of the tubulin polymers assembled after digestion with trypsin, Pronase, chymotrypsin, subtilisin, Staphylococcus aureus proteinase V8 and proteinase K were investigated. Digestion with trypsin, Pronase or chymotrypsin resulted in a decrease in the ability of tubulin for self-assembly, whereas limited proteolysis with subtilisin, S. aureus proteinase V8 or proteinase K resulted in an increase in such ability. The shape of the assembled polymers varied from typical microtubules (after the treatment with trypsin or Pronase) to sheets (after the treatment with chymotrypsin) and from hooked microtubules with a constant polarity (after the treatment with subtilisin) to the disappearance of a defined polarity of such polymers (after the treatment with S. aureus V8 proteinase or proteinase K). These results indicate that the tubulin C-terminal regions are involved in the regulation of microtubule polymerization, shape, directional growth and lateral interactions between tubulin protofilaments.
D002918:Chymotrypsin / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000494:pharmacology*; D007700:Kinetics; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D010446:Peptide Fragments / Q000032:analysis; D010449:Peptide Mapping; D011487:Protein Conformation / Q000187:drug effects; D012697:Serine Endopeptidases / Q000494:pharmacology; D013381:Subtilisins / Q000494:pharmacology; D014404:Tubulin / Q000378:metabolism*
D046911:Macromolecular Substances; D010446:Peptide Fragments; D014404:Tubulin; D010450:Endopeptidases; D012697:Serine Endopeptidases; D013381:Subtilisins; D002918:Chymotrypsin; C028344:glutamyl endopeptidase