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    Phylogenetic occurrence of coiled coil proteins: implications for tissue structure in metazoa via a coiled coil tissue matrix

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    Authors
    Odgren, Paul R.
    Harvie, Lawrence W.
    Fey, Edward G.
    UMass Chan Affiliations
    Department of Cell Biology
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    1996-04-01
    Keywords
    Animals; Bacterial Proteins; Cells, Cultured; Cervix Uteri; Database Management Systems; Epithelial Cells; Epithelium; Female; Humans; *Phylogeny; Plant Proteins; Protein Conformation; Viral Proteins
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    http://dx.doi.org/10.1002/(SICI)1097-0134(199604)24:4<467::AID-PROT6>3.0.CO;2-B
    Abstract
    We examined GenBank sequence files with a heptad repeat analysis program to assess the phylogenetic occurrence of coiled coil proteins, how heptad repeat domains are organized within them, and what structural/functional categories they comprise. Of 102,007 proteins analyzed, 5.95% (6,074) contained coiled coil domains; 1.26% (1,289) contained "extended" (> 75 amino acid) domains. While the frequency of proteins containing coiled coils was surprisingly constant among all biota, extended coiled coil proteins were fourfold more frequent in the animal kingdom and may reflect early events in the divergence of plants and animals. Structure/function categories of extended coils also revealed phylogenetic differences. In pathogens and parasites, many extended coiled coil proteins are external and bind host proteins. In animals, the majority of extended coiled coil proteins were identified as constituents of two protein categories: 1) myosins and motors; or 2) components of the nuclear matrix-intermediate filament scaffold. This scaffold, produced by sequential extraction of epithelial monolayers in situ, contains only 1-2% of the cell mass while accurately retaining morphological features of living epithelium and is greatly enriched in proteins with extensive, interrupted coiled coil forming domains. The increased occurrence of this type of protein in metazoa compared with plants or protists leads us to hypothesize a tissue-wide matrix of coiled coil interactions underlying metazoan differentiated cell and tissue structure.
    Source
    Proteins. 1996 Apr;24(4):467-84. Link to article on publisher's site
    DOI
    10.1002/(SICI)1097-0134(199604)24:4<467::AID-PROT6>3.0.CO;2-B
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/34260
    PubMed ID
    9162947
    Related Resources
    Link to article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1002/(SICI)1097-0134(199604)24:4<467::AID-PROT6>3.0.CO;2-B
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