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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
50
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pubmed:dateCreated |
1997-1-17
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pubmed:abstractText |
Mammalian brain cytoplasmic dynein contains three light chains of Mr = 8,000, 14,000, and 22,000 (King, S. M., Barbarese, E., Dillman, J. F., III, Patel-King, R. S., Carson, J. H., and Pfister, K. K. (1996) J. Biol. Chem. 271, 19358-19366). Peptide sequence data (16/16 residues correct) implicate the Mr = 14,000 polypeptide as Tctex-1, a protein encoded within the mouse t-complex. Tctex-1 cosediments with microtubules and is eluted with ATP or salt but not with GTP as expected for a dynein subunit. The ATP-eluted protein precisely cosediments with known cytoplasmic dynein proteins in sucrose density gradients. Tctex-1 also is immunoprecipitated from brain and other tissue homogenates by a monoclonal antibody raised against the 74-kDa cytoplasmic dynein intermediate chain. Quantitative densitometry indicates that Tctex-1 is a stoichiometric component of the dynein complex. As Tctex-1 is a candidate for involvement in the transmission ratio distortion (meiotic drive) of mouse t-haplotypes, these results suggest that cytoplasmic dynein dysfunction may play an important role in non-mendelian chromosome segregation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chaperonin Containing TCP-1,
http://linkedlifedata.com/resource/pubmed/chemical/Chaperonins,
http://linkedlifedata.com/resource/pubmed/chemical/Dyneins,
http://linkedlifedata.com/resource/pubmed/chemical/Maltose-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
271
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
32281-7
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:8943288-Amino Acid Sequence,
pubmed-meshheading:8943288-Animals,
pubmed-meshheading:8943288-Bacterial Proteins,
pubmed-meshheading:8943288-Brain Chemistry,
pubmed-meshheading:8943288-Carrier Proteins,
pubmed-meshheading:8943288-Centrifugation, Density Gradient,
pubmed-meshheading:8943288-Chaperonin Containing TCP-1,
pubmed-meshheading:8943288-Chaperonins,
pubmed-meshheading:8943288-Dyneins,
pubmed-meshheading:8943288-Maltose-Binding Proteins,
pubmed-meshheading:8943288-Membrane Proteins,
pubmed-meshheading:8943288-Mice,
pubmed-meshheading:8943288-Molecular Sequence Data,
pubmed-meshheading:8943288-Molecular Weight,
pubmed-meshheading:8943288-Sequence Alignment
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pubmed:year |
1996
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pubmed:articleTitle |
The mouse t-complex-encoded protein Tctex-1 is a light chain of brain cytoplasmic dynein.
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pubmed:affiliation |
Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06032-3305, USA. king@panda.uchc.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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