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dc.contributor.authorPereira, Andrea J.
dc.contributor.authorDalby, Brian
dc.contributor.authorStewart, Russell J.
dc.contributor.authorDoxsey, Stephen J.
dc.contributor.authorGoldstein, Lawrence S. B.
dc.date2022-08-11T08:10:05.000
dc.date.accessioned2022-08-23T16:54:56Z
dc.date.available2022-08-23T16:54:56Z
dc.date.issued1997-03-10
dc.date.submitted2008-08-15
dc.identifier.citationJ Cell Biol. 1997 Mar 10;136(5):1081-90.
dc.identifier.issn0021-9525 (Print)
dc.identifier.pmid9060472
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42611
dc.description.abstractThe kinesin superfamily is a large group of proteins (kinesin-like proteins [KLPs]) that share sequence similarity with the microtubule (MT) motor kinesin. Several members of this superfamily have been implicated in various stages of mitosis and meiosis. Here we report our studies on KLP67A of Drosophila. DNA sequence analysis of KLP67A predicts an MT motor protein with an amino-terminal motor domain. To prove this directly, KLP67A expressed in Escherichia coli was shown in an in vitro motility assay to move MTs in the plus direction. We also report expression analyses at both the mRNA and protein level, which implicate KLP67A in the localization of mitochondria in undifferentiated cell types. In situ hybridization studies of the KLP67A mRNA during embryogenesis and larval central nervous system development indicate a proliferation-specific expression pattern. Furthermore, when affinity-purified anti-KLP67A antisera are used to stain blastoderm embryos, mitochondria in the region of the spindle asters are labeled. These data suggest that KLP67A is a mitotic motor of Drosophila that may have the unique role of positioning mitochondria near the spindle.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=9060472&dopt=Abstract">Link to Article in PubMed</a>
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectBase Sequence
dc.subjectCHO Cells
dc.subjectCricetinae
dc.subjectDNA, Complementary
dc.subjectDrosophila
dc.subject*Drosophila Proteins
dc.subjectEscherichia coli
dc.subjectGene Expression Regulation, Developmental
dc.subjectMicrotubule-Associated Proteins
dc.subjectpurification
dc.subjectMicrotubules
dc.subjectMitochondria
dc.subjectMitosis
dc.subjectMolecular Sequence Data
dc.subjectRNA, Messenger
dc.subjectRecombinant Fusion Proteins
dc.subjectCell Biology
dc.titleMitochondrial association of a plus end-directed microtubule motor expressed during mitosis in Drosophila
dc.typeJournal Article
dc.source.journaltitleThe Journal of cell biology
dc.source.volume136
dc.source.issue5
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1942&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/943
dc.identifier.contextkey579833
refterms.dateFOA2022-08-23T16:54:56Z
html.description.abstract<p>The kinesin superfamily is a large group of proteins (kinesin-like proteins [KLPs]) that share sequence similarity with the microtubule (MT) motor kinesin. Several members of this superfamily have been implicated in various stages of mitosis and meiosis. Here we report our studies on KLP67A of Drosophila. DNA sequence analysis of KLP67A predicts an MT motor protein with an amino-terminal motor domain. To prove this directly, KLP67A expressed in Escherichia coli was shown in an in vitro motility assay to move MTs in the plus direction. We also report expression analyses at both the mRNA and protein level, which implicate KLP67A in the localization of mitochondria in undifferentiated cell types. In situ hybridization studies of the KLP67A mRNA during embryogenesis and larval central nervous system development indicate a proliferation-specific expression pattern. Furthermore, when affinity-purified anti-KLP67A antisera are used to stain blastoderm embryos, mitochondria in the region of the spindle asters are labeled. These data suggest that KLP67A is a mitotic motor of Drosophila that may have the unique role of positioning mitochondria near the spindle.</p>
dc.identifier.submissionpathoapubs/943
dc.contributor.departmentProgram in Molecular Medicine
dc.source.pages1081-90


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