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dc.contributor.authorWilkerson, Curtis G.
dc.contributor.authorKing, Stephen M.
dc.contributor.authorWitman, George B.
dc.date2022-08-11T08:08:04.000
dc.date.accessioned2022-08-23T15:41:08Z
dc.date.available2022-08-23T15:41:08Z
dc.date.issued1994-03-01
dc.date.submitted2008-12-11
dc.identifier.citationJ Cell Sci. 1994 Mar;107 ( Pt 3):497-506.
dc.identifier.issn0021-9533 (Print)
dc.identifier.pmid7516341
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26563
dc.description.abstractWe report here the complete sequence of the gamma dynein heavy chain of the outer arm of the Chlamydomonas flagellum, and partial sequences for six other dynein heavy chains. The gamma dynein heavy chain sequence contains four P-loop motifs, one of which is the likely hydrolytic site based on its position relative to a previously mapped epitope. Comparison with available cytoplasmic and flagellar dynein heavy chain sequences reveals regions that are highly conserved in all dynein heavy chains sequenced to date, regions that are conserved only among axonemal dynein heavy chains, and regions that are unique to individual dynein heavy chains. The presumed hydrolytic site is absolutely conserved among dyneins, two other P loops are highly conserved among cytoplasmic dynein heavy chains but not in axonemal dynein heavy chains, and the fourth P loop is invariant in axonemal dynein heavy chains but not in cytoplasmic dynein. One region that is very highly conserved in all dynein heavy chains is similar to a portion of the ATP-sensitive microtubule-binding domain of kinesin. Two other regions present in all dynein heavy chains are predicted to have high alpha-helical content and have a high probability of forming coiled-coil structures. Overall, the central one-third of the gamma dynein heavy chain is most conserved whereas the N-terminal one-third is least conserved; the fact that the latter region is divergent between the cytoplasmic dynein heavy chain and two different axonemal dynein heavy chains suggests that it is involved in chain-specific functions.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=7516341&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://jcs.biologists.org/cgi/content/abstract/107/3/497
dc.subjectAdenosine Triphosphate
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectBase Sequence
dc.subjectChlamydomonas
dc.subjectCloning, Molecular
dc.subjectDNA
dc.subjectDynein ATPase
dc.subjectEpitopes
dc.subjectFlagella
dc.subjectKinesin
dc.subjectMicrotubules
dc.subjectMolecular Sequence Data
dc.subjectSequence Homology, Amino Acid
dc.subjectCell Biology
dc.titleMolecular analysis of the gamma heavy chain of Chlamydomonas flagellar outer-arm dynein
dc.typeJournal Article
dc.source.journaltitleJournal of cell science
dc.source.volume107 ( Pt 3)
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/cellbiology_pp/7
dc.identifier.contextkey680149
html.description.abstract<p>We report here the complete sequence of the gamma dynein heavy chain of the outer arm of the Chlamydomonas flagellum, and partial sequences for six other dynein heavy chains. The gamma dynein heavy chain sequence contains four P-loop motifs, one of which is the likely hydrolytic site based on its position relative to a previously mapped epitope. Comparison with available cytoplasmic and flagellar dynein heavy chain sequences reveals regions that are highly conserved in all dynein heavy chains sequenced to date, regions that are conserved only among axonemal dynein heavy chains, and regions that are unique to individual dynein heavy chains. The presumed hydrolytic site is absolutely conserved among dyneins, two other P loops are highly conserved among cytoplasmic dynein heavy chains but not in axonemal dynein heavy chains, and the fourth P loop is invariant in axonemal dynein heavy chains but not in cytoplasmic dynein. One region that is very highly conserved in all dynein heavy chains is similar to a portion of the ATP-sensitive microtubule-binding domain of kinesin. Two other regions present in all dynein heavy chains are predicted to have high alpha-helical content and have a high probability of forming coiled-coil structures. Overall, the central one-third of the gamma dynein heavy chain is most conserved whereas the N-terminal one-third is least conserved; the fact that the latter region is divergent between the cytoplasmic dynein heavy chain and two different axonemal dynein heavy chains suggests that it is involved in chain-specific functions.</p>
dc.identifier.submissionpathcellbiology_pp/7
dc.contributor.departmentDepartment of Cell Biology
dc.source.pages497-506


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