Microtubule Assembly in the Absence of Added Nucleotides

Microtubule Assembly in the Absence of Added Nucleotides

Vol. 70, No. 3, pp. 765–768, March 1973 | MICHAEL L. SHELANSKI*, FELICIA GASKIN†, AND CHARLES R. CANTOR†
The study investigates the assembly of microtubules in the absence of added nucleotides, focusing on the effects of sucrose and glycerol. The researchers found that both sucrose and glycerol significantly enhance the assembly of tubulin, a protein essential for microtubule formation. Tubules assembled in glycerol and sucrose are more stable than those formed without these compounds. Assembly can occur in the absence of ATP or GTP but is accelerated by their presence. The study also demonstrates that tubulin can be purified through a process involving assembly and disassembly in glycerol-containing solutions, yielding a highly pure form of the protein. The stability of microtubules in glycerol is further highlighted, as they remain stable at low temperatures and are resistant to colchicine. The findings suggest that glycerol and sucrose may preserve the structural integrity of tubulin, potentially facilitating protein studies and long-term storage. Additionally, the study explores the role of nucleotides in microtubule assembly, noting that while GTP accelerates assembly, it may serve a regulatory function by stabilizing tubulin against thermal denaturation. The presence of abnormal assembly forms under various conditions indicates potential errors in the assembly process, which may be more pronounced under rapid assembly conditions.The study investigates the assembly of microtubules in the absence of added nucleotides, focusing on the effects of sucrose and glycerol. The researchers found that both sucrose and glycerol significantly enhance the assembly of tubulin, a protein essential for microtubule formation. Tubules assembled in glycerol and sucrose are more stable than those formed without these compounds. Assembly can occur in the absence of ATP or GTP but is accelerated by their presence. The study also demonstrates that tubulin can be purified through a process involving assembly and disassembly in glycerol-containing solutions, yielding a highly pure form of the protein. The stability of microtubules in glycerol is further highlighted, as they remain stable at low temperatures and are resistant to colchicine. The findings suggest that glycerol and sucrose may preserve the structural integrity of tubulin, potentially facilitating protein studies and long-term storage. Additionally, the study explores the role of nucleotides in microtubule assembly, noting that while GTP accelerates assembly, it may serve a regulatory function by stabilizing tubulin against thermal denaturation. The presence of abnormal assembly forms under various conditions indicates potential errors in the assembly process, which may be more pronounced under rapid assembly conditions.
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