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J Struct Biol. 1990 Oct-Dec;105(1-3):46-53.

Isoforms of tau protein from mammalian brain and avian erythrocytes: structure, self-assembly, and elasticity.

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Max-Planck-Unit for Structural Molecular Biology, DESY, Hamburg, Federal Republic of Germany.


Previous studies on tau protein showed that the protein forms paracrystals which are unusually elastic. The paracrystals were obtained from a mixture of isoforms prepared from brain tissue, and the protein was in a mixed state of phosphorylation. Subsequently we showed that the structure and elasticity was related to the state of phosphorylation. However, this left open the possibility that the isotype composition played a role as well. We have now addressed this question by separating the individual isoforms and analyzing their structure. The paracrystals from all isoforms are similar to one another and to those of the native mixture; the same holds for the elasticity. Thus the tendency to self-associate, the apparent structure, and the elasticity are determined by those regions of tau which all isoforms have in common. In addition we compare tau paracrystals from three different sources. Apart from the porcine brain tau described earlier we have prepared paracrystals from bovine brain tau because its sequence is now known (Himmler et al., 1989). The structure and elasticity is indistinguishable from porcine tau. Second, we have prepared tau from avian erythrocytes where it is found in the membrane-associated marginal band microtubules (Murphy and Wallis, 1985). Its isoform composition differs from mammalian brain tau, but again the structural properties are similar. A notable difference is that the shift in electrophoretic mobility induced by phosphorylation with CaM kinase, typical of all brain tau isotypes, is not found in the marginal band tau. Tau shows a strong tendency of longitudinal self-association which is apparent not only in the crystallization buffer but also in standard microtubule reassembly buffer.(ABSTRACT TRUNCATED AT 250 WORDS).

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