Literature DB >> 2958487

Dynein structure and function.

K A Johnson1, S P Marchese-Ragona, D B Clutter, E L Holzbaur, T J Chilcote.   

Abstract

The structure of dynein isolated from several sources follows the pattern first observed with Tetrahymena 22S dynein, which has three globular heads attached by three flexible strands to a root-like base. Recent biochemical data indicate that there is one ATPase site on each dynein head and that all three heads interact with microtubules in an ATP-sensitive manner. Accordingly, images of dynein in situ can be interpreted in terms of a model for crossbridge action where the roots of the bouquet anchor the dynein to the A-tubule and all three heads reach out to interact with the B-tubule in an ATP-dependent reaction to produce a force for sliding.

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Year:  1986        PMID: 2958487     DOI: 10.1242/jcs.1986.supplement_5.12

Source DB:  PubMed          Journal:  J Cell Sci Suppl        ISSN: 0269-3518


  3 in total

1.  Measurement of the force produced by an intact bull sperm flagellum in isometric arrest and estimation of the dynein stall force.

Authors:  K A Schmitz; D L Holcomb-Wygle; D J Oberski; C B Lindemann
Journal:  Biophys J       Date:  2000-07       Impact factor: 4.033

2.  Isolation of dynein heavy chain cDNAs from trout testis which predict an extensive carboxyl-terminal alpha-helical coiled-coil domain.

Authors:  A T Garber; J D Retief; G H Dixon
Journal:  EMBO J       Date:  1989-06       Impact factor: 11.598

3.  The Kinetics of Nucleotide Binding to Isolated Chlamydomonas Axonemes Using UV-TIRF Microscopy.

Authors:  Maria Feofilova; Mohammed Mahamdeh; Jonathon Howard
Journal:  Biophys J       Date:  2019-07-09       Impact factor: 4.033

  3 in total

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