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dc.contributor.authorKoutoulis, Anthony
dc.contributor.authorPazour, Gregory J.
dc.contributor.authorWilkerson, Curtis G.
dc.contributor.authorInaba, Kazuo
dc.contributor.authorSheng, Hong
dc.contributor.authorTakada, Saeko
dc.contributor.authorWitman, George B.
dc.date2022-08-11T08:08:03.000
dc.date.accessioned2022-08-23T15:40:53Z
dc.date.available2022-08-23T15:40:53Z
dc.date.issued1997-06-02
dc.date.submitted2008-12-11
dc.identifier.citation<p>J Cell Biol. 1997 Jun 2;137(5):1069-80.</p>
dc.identifier.issn0021-9525 (Print)
dc.identifier.doi10.1083/jcb.137.5.1069
dc.identifier.pmid9166407
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26503
dc.description.abstractWe have used an insertional mutagenesis/ gene tagging technique to generate new Chlamydomonas reinhardtii mutants that are defective in assembly of the uter ynein rm. Among 39 insertional oda mutants characterized, two are alleles of the previously uncloned ODA3 gene, one is an allele of the uncloned ODA10 gene, and one represents a novel ODA gene (termed ODA12). ODA3 is of particular interest because it is essential for assembly of both the outer dynein arm and the outer dynein arm docking complex (ODA-DC) onto flagellar doublet microtubules (Takada, S., and R. Kamiya. 1994. J. Cell Biol. 126:737- 745). Beginning with the inserted DNA as a tag, the ODA3 gene and a full-length cDNA were cloned. The cloned gene rescues the phenotype of oda3 mutants. The cDNA sequence predicts a novel 83. 4-kD protein with extensive coiled-coil domains. The ODA-DC contains three polypeptides; direct amino acid sequencing indicates that the largest of these polypeptides corresponds to ODA3. This protein is likely to have an important role in the precise positioning of the outer dynein arms on the flagellar axoneme.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=9166407&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2136212
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectBase Sequence
dc.subjectChlamydomonas reinhardtii
dc.subjectCloning, Molecular
dc.subjectDNA, Complementary
dc.subjectDNA, Plant
dc.subjectDynein ATPase
dc.subjectFlagella
dc.subjectGenes, Plant
dc.subjectMolecular Sequence Data
dc.subjectMutagenesis, Insertional
dc.subjectSequence Analysis, DNA
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectCell Biology
dc.subjectGenetic Phenomena
dc.titleThe Chlamydomonas reinhardtii ODA3 gene encodes a protein of the outer dynein arm docking complex
dc.typeArticle
dc.source.journaltitleThe Journal of cell biology
dc.source.volume137
dc.source.issue5
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/cellbiology_pp/19
dc.identifier.contextkey680161
html.description.abstract<p>We have used an insertional mutagenesis/ gene tagging technique to generate new Chlamydomonas reinhardtii mutants that are defective in assembly of the uter ynein rm. Among 39 insertional oda mutants characterized, two are alleles of the previously uncloned ODA3 gene, one is an allele of the uncloned ODA10 gene, and one represents a novel ODA gene (termed ODA12). ODA3 is of particular interest because it is essential for assembly of both the outer dynein arm and the outer dynein arm docking complex (ODA-DC) onto flagellar doublet microtubules (Takada, S., and R. Kamiya. 1994. J. Cell Biol. 126:737- 745). Beginning with the inserted DNA as a tag, the ODA3 gene and a full-length cDNA were cloned. The cloned gene rescues the phenotype of oda3 mutants. The cDNA sequence predicts a novel 83. 4-kD protein with extensive coiled-coil domains. The ODA-DC contains three polypeptides; direct amino acid sequencing indicates that the largest of these polypeptides corresponds to ODA3. This protein is likely to have an important role in the precise positioning of the outer dynein arms on the flagellar axoneme.</p>
dc.identifier.submissionpathcellbiology_pp/19
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentDepartment of Cell Biology
dc.source.pages1069-80


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