ISSN:
0275-3723
Keywords:
microtubule protein
;
tubulin-sheets
;
zinc
;
MAPs
;
tubulin lateral interaction
;
Chemistry
;
Molecular Cell Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
Addition of increasing amounts of zinc to a cold microtubule protein solution results in the disappearance of 30 S oligomer found in the absence of that cation and in the appearance of new tubulin oligomers, 90 S and 23 S. When a microtubule protein solution is warmed in the presence of zinc, tubulin-sheets are assembled. We have tested the influence of microtubule associated proteins and the zinc:tubulin ratio on the polymerization process. Depletion of microtubule associated proteins results in wider and longer tubulin-sheets than those polymerized in the presence of microtubule associated proteins. However by increasing zinc concentration wider but shorter tubulin-sheets were found. These results suggest that microtubule associated proteins and zinc could promote nucleation of tubulin-sheets, but zinc also promotes lateral tubulin-tubulin interaction. This interpretation was confirmed when microtubule protein was assembled at a low zinctubulin ratio. In such conditions composite structures of microtubules and zinc tubulin-sheets arc formed. These composite structures are consequence of a lateral attachment of a zinc tubulin-sheet on a microtubule protofilament.
Additional Material:
8 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/jsscb.380170208
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