Axonemal dyneins and cytoplasmic dynein have evolved separate strategies to perform their tasks. The multi-dynein hypothesis accurately describes the highly specialized axonemal isoforms; each isoform is encoded by a separate gene, is located in a precise place, produces specific forces which contri
Dynein and dynein-related genes
โ Scribed by Milisav, Irina
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 75 KB
- Volume
- 39
- Category
- Article
- ISSN
- 0886-1544
No coin nor oath required. For personal study only.
โฆ Synopsis
Dyneins are large, multisubunit ATPases that interact with microtubules to generate force. Dyneins move eukaryotic cilia and flagella and are in the cytoplasm, where they are involved in the transport of particles and organelles along microtubules and in the transport of condensed chromosomes during mitosis [reviewed in Holzbaur et al., 1994;Gibbons, 1996]. Defects in human axonemal dynein complexes have been shown to be associated with Kartagener's syndrome, which is characterized by recurrent respiratory tract infections, immotile sperm and situs inversus. Cytoplasmic and axonemal dyneins are composed of heavy, intermediate, and light chains. The best characterised groups of dynein genes so far are those encoding cytoplasmic heavy chains and heavy chains from the outer arms from axonemes. These share extensive sequence similarity and are conserved throughout species. Recently, several genes encoding intermediate and light chains have been identified; these have encoded a remarkable diversity of products, which also seem to be highly conserved between species, although they fall into several complex groups. The structure of dynein heavy chain genes, the emerging knowledge on intermediate and light chain genes and their products, and the possible involvement of dyneins in disease are discussed.
๐ SIMILAR VOLUMES
Flagellar outer row dynein ATPases have been used extensively as model systems for studies of microtubule-based motility. Previously full-length sequences were only available for two of the three catalytic heavy-chain subunits (DHCs) of this enzyme. We have completed the sequence of an 18-kb genomic