Linked Life Data

7706400

Source:http://linkedlifedata.com/resource/pubmed/id/7706400

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pubmed-article:7706400pubmed:abstractTextThe CHO1 antigen is a mitosis-specific kinesin-like motor located at the interzonal region of the spindle. The human cDNA coding for the antigen contains a domain with sequence similarity to the motor domain of kinesin-like protein (Nislow et al., Nature 359, 543, 1992). Here we cloned cDNAs encoding the CHO1 antigen by immunoscreening of a CHO Uni-Zap expression library, the same species in which the original monoclonal antibody was raised. cDNAs of CHO cells encode a 953 amino acid polypeptide with a calculated molecular mass of 109 kDa. The N-terminal 73% of the antigen was 87% identical to the human clone, whereas the remaining 27% of the coding region showed only 48% homology. Insect Sf9 cells infected with baculovirus containing the full-length insert produced 105 and 95 kDa polypeptides, the same doublet identified as the original antigen in CHO cells. Truncated polypeptides corresponding to the N-terminal motor and C-terminal tail produced a 56 and 54 kDa polypeptide in Sf9 cells, respectively. Full and N-terminal proteins co-sedimented with, and caused bundling of, brain microtubules in vitro, whereas the C-terminal polypeptide did not. Cells expressing the N terminus formed one or more cytoplasmic processes. Immunofluorescence as well as electron microscopic observations revealed the presence of thick bundles of microtubules, which were closely packed, forming a marginal ring just beneath the cell membrane and a core in the processes. The diffusion coefficient and sedimentation coefficient were determined for the native CHO1 antigen by gel filtration and sucrose density gradient centrifugation, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)lld:pubmed
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pubmed-article:7706400pubmed:volume107 ( Pt 12)lld:pubmed
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pubmed-article:7706400pubmed:articleTitleHeterogeneity and microtubule interaction of the CHO1 antigen, a mitosis-specific kinesin-like protein. Analysis of subdomains expressed in insect sf9 cells.lld:pubmed
pubmed-article:7706400pubmed:affiliationDepartment of Cell Biology and Neuroanatomy, University of Minnesota, Minneapolis 55455.lld:pubmed
pubmed-article:7706400pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7706400pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:7706400pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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