| Literature DB >> 9786086 |
Abstract
In Allogromia, tubulin lattices transform between microtubule and helical filament states. Helical filaments are composed of approximately 10-nm-thick tubulin filaments wound into approximately 30-nm diameter coils. The transition pathway between these two lattice states was examined in vitro in detergent-lysed pseudopods. Microtubules represented the majority of the assembled tubulin polymers in the detergent extracted pseudopodia. However, microtubules transformed into helical filaments upon exposure to 10 mM Ca2+ or 50 mM Mg2+. The conversion of microtubules into helical filaments involved fragmentation of the tubulin lattice and reduction in total polymer length. Divalent cations were required for the maintenance of the helical filament state; their removal resulted in the loss of helical filaments and the re-formation of microtubules. The data support a direct transition model in which the tubulin lattice interconverts between the helical filament and microtubule states, independently of tubulin subunit concentration. We propose a structural model for the direct pathway whereby disruption of longitudinal bonds between tandem tubulin dimers in protofilaments causes the microtubule lattice to unwind into helical filaments--continuous ribbons of laterally connected tubulin dimers--from the microtubule end. Helical filaments may rewind into microtubules as longitudinal intersubunit bonds reform.Entities:
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Year: 1998 PMID: 9786086 DOI: 10.1002/(SICI)1097-0169(1998)41:2<107::AID-CM2>3.0.CO;2-B
Source DB: PubMed Journal: Cell Motil Cytoskeleton ISSN: 0886-1544