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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1995-5-11
|
| pubmed:databankReference | |
| pubmed:abstractText |
The 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)
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0021-9533
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
107 ( Pt 12)
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
3485-99
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:7706400-Amino Acid Sequence,
pubmed-meshheading:7706400-Animals,
pubmed-meshheading:7706400-Base Sequence,
pubmed-meshheading:7706400-CHO Cells,
pubmed-meshheading:7706400-Cells, Cultured,
pubmed-meshheading:7706400-Cloning, Molecular,
pubmed-meshheading:7706400-Cricetinae,
pubmed-meshheading:7706400-HeLa Cells,
pubmed-meshheading:7706400-Humans,
pubmed-meshheading:7706400-Kinesin,
pubmed-meshheading:7706400-Microtubule-Associated Proteins,
pubmed-meshheading:7706400-Microtubules,
pubmed-meshheading:7706400-Mitosis,
pubmed-meshheading:7706400-Molecular Sequence Data,
pubmed-meshheading:7706400-Peptide Fragments,
pubmed-meshheading:7706400-Protein Binding,
pubmed-meshheading:7706400-Recombinant Proteins,
pubmed-meshheading:7706400-Sequence Analysis, DNA,
pubmed-meshheading:7706400-Sequence Homology, Amino Acid,
pubmed-meshheading:7706400-Spodoptera,
pubmed-meshheading:7706400-Structure-Activity Relationship
|
| pubmed:year |
1994
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| pubmed:articleTitle |
Heterogeneity and microtubule interaction of the CHO1 antigen, a mitosis-specific kinesin-like protein. Analysis of subdomains expressed in insect sf9 cells.
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| pubmed:affiliation |
Department of Cell Biology and Neuroanatomy, University of Minnesota, Minneapolis 55455.
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|