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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1999-1-21
|
| pubmed:abstractText |
The cortex of ciliates, dinoflagellates and euglenoids comprises a unique structure called the epiplasm, implicated in pattern-forming processes of the cell cortex and in maintaining cell shape. Despite significant variation in the structural organization of their epiplasm and cortex, a novel type of cytoskeletal protein named articulin is the principal constituent of the epiplasm in the euglenoid Euglena and the ciliate Pseudomicrothorax. For another ciliate, Paramecium, epiplasmins, a group of polypeptides with common biochemical properties, are the major constituents of the epiplasm. Using molecular tools and affinity purification we have selected polyclonal antibodies and identified epitopes of monoclonal antibodies that identify epitopes characteristic of articulins and epiplasmins. With these antibodies we have analysed the occurrence of the two types of cytoskeletal proteins in a dinoflagellate, a euglenoid and several ciliates. Our results indicate that both articulins and epiplasmins are present in these organisms, suggesting that both contribute to the organization of the membrane skeleton in protists. Articulins and epiplasmins represent two distinct classes of cytoskeletal proteins, since different polypeptides were labeled by articulin core domain-specific or epiplasmin epitope-specific antibodies in each organism studied. In one case, a polypeptide in Pseudomicrothorax was identified that reacts with both articulin core domain-specific and with anti-epiplasmin monoclonal antibodies; however, the epiplasmin monoclonal antibody epitope was mapped to the C terminus of the polypeptide, well outside the central VPV-repeat core domain that contains the articulin monoclonal antibody epitope and that is the hallmark of the articulins.
|
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/articulin
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
0021-9533
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
111 ( Pt 22)
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
3367-78
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9788878-Amino Acid Sequence,
pubmed-meshheading:9788878-Animals,
pubmed-meshheading:9788878-Bacterial Proteins,
pubmed-meshheading:9788878-Ciliophora,
pubmed-meshheading:9788878-Cross Reactions,
pubmed-meshheading:9788878-Cytoskeletal Proteins,
pubmed-meshheading:9788878-Dinoflagellida,
pubmed-meshheading:9788878-Epitope Mapping,
pubmed-meshheading:9788878-Epitopes,
pubmed-meshheading:9788878-Euglena gracilis,
pubmed-meshheading:9788878-Gene Expression,
pubmed-meshheading:9788878-Klebsiella pneumoniae,
pubmed-meshheading:9788878-Membrane Proteins,
pubmed-meshheading:9788878-Molecular Sequence Data,
pubmed-meshheading:9788878-Paramecium tetraurelia,
pubmed-meshheading:9788878-Plasmids,
pubmed-meshheading:9788878-Protozoan Proteins,
pubmed-meshheading:9788878-Tetrahymena pyriformis
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| pubmed:year |
1998
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| pubmed:articleTitle |
Articulins and epiplasmins: two distinct classes of cytoskeletal proteins of the membrane skeleton in protists.
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| pubmed:affiliation |
Max Planck Institute for Biophysical Chemistry, Department of Biochemistry, Am Fassberg 11, D-37077 Göttingen, Germany.
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|