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Assembly of microtubules with ATP: evidence that only a fraction of the protein is assembly‐competent
Author(s) -
Islam Khalid,
Burns Roy G.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80613-4
Subject(s) - gtp' , microtubule , phosphorylation , microbiology and biotechnology , incubation , biophysics , tubulin , guanosine triphosphate , chemistry , biochemistry , microtubule associated protein , adenosine triphosphate , protein kinase a , biology , enzyme
Chick brain microtubule protein can be assembled in vitro with ATP, although the extent of assembly is less than that with GTP. The ATP‐induced assembly is not the result of generation of GTP by the co‐purifying nucleoside diphosphate kinase. Neither an observed increase in the critical concentration nor the phosphorylation of MAP2 can account for the decreased extent of assembly. However, whereas microtubules are formed with both ATP and GTP, incubation with ATP yields additional filaments and polymorphic aggregates. The results demonstrate that of the total protein which can be assembled into microtubules by GTP, about 25–35% is assembled into other structural forms in the presence of ATP.