Microdensitometer—computer correlation analysis of two distinct, spatially segregated classes of microtubule bridges in Allogromia pseudopodia

Previous video-light microscopic studies have shown that the microtubule bundles in the pseudopodia of foraminiferan protists display several types of movements in vivo, including active bending, zipping/splaying, and axial translocations. To gain insight into the types and arrangement of microtubul...

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Veröffentlicht in:Journal of structural biology 1990-10, Vol.105 (1), p.1-10
Hauptverfasser: Jensen, C.G., Bollard, S.M., Jensen, L.C.W., Travis, J.L., Bowser, S.S.
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Sprache:eng
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Zusammenfassung:Previous video-light microscopic studies have shown that the microtubule bundles in the pseudopodia of foraminiferan protists display several types of movements in vivo, including active bending, zipping/splaying, and axial translocations. To gain insight into the types and arrangement of microtubule-associated proteins ( e.g., mechanoenzymes, crosslinkers) in such a highly dynamic system, we employed microdensitometric-computer correlation methods to analyze, quantitatively, intermicrotubule bridges in thin-section electron micrographs of Allogromia laticollaris and Allogromia sp. (strain NF). Two distinct bridges occupying mutually exclusive zones between adjacent microtubules were identified. Type I bridges displayed a single axial repeat (34 nm for A. laticollaris and 28 nm for Allogromia sp.) and Type II bridges showed a typical 12-dimer helical superlattice pattern. In A. laticollaris, the two types of bridges were morphologically distinct: Type I bridges were aligned perpendicular to the microtubule wall and were 23-nm wide with an electron-lucent core; Type II bridges were irregular filaments projecting from the microtubules at various angles. When compared with the known distribution of microtubule-associated proteins in other systems, our findings indicate that, in viuo, Allogromia pseudopodial microtubules are decorated with MAP2-like bridges interrupted by discrete clusters of a dynein-like component.
ISSN:1047-8477
1095-8657
DOI:10.1016/1047-8477(90)90092-Q