Interspecies conservation of outer arm dynein intermediate chain sequences defines two intermediate chain subclasses.
Open Access
- 1 June 1995
- journal article
- Published by American Society for Cell Biology (ASCB) in Molecular Biology of the Cell
- Vol. 6 (6) , 685-696
- https://doi.org/10.1091/mbc.6.6.685
Abstract
Immunological analysis showed that antibodies against the intermediate chains (ICs) IC2 and IC3 of sea urchin outer arm dynein specifically cross-reacted with intermediate chains IC78 and IC69, respectively, of Chlamydomonas outer arm dynein. In contrast, no specific cross-reactivity with any Chlamydomonas outer arm polypeptide was observed using antibody against IC1 of sea urchin outer arm dynein. To learn more about the relationships between the different ICs, overlapping cDNAs encoding all of IC2 and IC3 of sea urchin were isolated and sequenced. Comparison of these sequences with those previously obtained for the Chlamydomonas ICs revealed that, although all four chains are homologous, sea urchin IC2 is much more closely related to Chlamydomonas IC78 (45.8% identity), and sea urchin IC3 is much more closely related to Chlamydomonas IC69 (48.5% identity), than either sea urchin chain is related to the other (23.5% identity). For homologous pairs, the similarities extend throughout the full lengths of the chains. Regions of similarity between all four ICs and the IC (IC74) of cytoplasmic dynein, located in the C-terminal halves of the chains, are due primarily to conservation of the WD repeats present in all of these ICs. This is the first demonstration that structural differences between individual ICs within an outer arm dynein have been highly conserved in the dyneins of distantly related species. The results provide a basis for the subclassification of these chains.Keywords
This publication has 27 references indexed in Scilit:
- The alpha subunit of sea urchin sperm outer arm dynein mediates structural and rigor binding to microtubules.The Journal of cell biology, 1992
- Extragenic suppressors of paralyzed flagellar mutations in Chlamydomonas reinhardtii identify loci that alter the inner dynein arms.The Journal of cell biology, 1992
- Homology of the 74-kD cytoplasmic dynein subunit with a flagellar dynein polypeptide suggests an intracellular targeting function.The Journal of cell biology, 1992
- The WD‐40 repeatFEBS Letters, 1992
- Identification of oda6 as a Chlamydomonas dynein mutant by rescue with the wild-type gene.The Journal of cell biology, 1991
- The Mr 78,000 intermediate chain of Chlamydomonas outer arm dynein interacts with alpha-tubulin in situJournal of Biological Chemistry, 1991
- Microtubule binding and translocation by inner dynein arm subtype i1Cell Motility, 1991
- Localization of an intermediate chain of outer arm dynein by immunoelectron microscopy.Journal of Biological Chemistry, 1990
- OUTER ARM DYNEIN FROM TROUT SPERMATOZOA - PURIFICATION, POLYPEPTIDE COMPOSITION, AND ENZYMTIC PROPERTIES1989
- Mutations at twelve independent loci result in absence of outer dynein arms in Chylamydomonas reinhardtii.The Journal of cell biology, 1988