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    Sequence-divergent units of the ABA-1 polyprotein array of the nematode Ascaris suum have similar fatty-acid- and retinol-binding properties but different binding-site environments

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    Authors
    Moore, Joyce
    McDermott, Lindsay C.
    Price, Nicholas C.
    Kelly, Sharon M.
    Cooper, Alan
    Kennedy, Malcolm W.
    Issue Date
    1999-05-15
    Subjects
    n-3 polyunsaturated fatty acids
    C700 Molecular Biology, Biophysics and Biochemistry
    
    Metadata
    Show full item record
    Abstract
    Polyproteins comprise long polypeptides that are post-translationally cleaved into proteins of different function, or tandemly repetitive polypeptides which are processed into multiple versions of proteins which are presumed to have the same function. In the latter case the individual units of the polyprotein can differ substantially in sequence. Identity of function between the different units therefore cannot be assumed. Here we have examined the ABA-1 polyprotein allergen of the parasitic nematode Ascaris suum and found it to contain units which show a 50% difference in amino acid sequence. The parasite therefore produces at least two radically different forms of the allergen encoded within the polyprotein array. In fluorescence-based ligand-binding assays, recombinant polypeptides representing the two forms (designated ABA-1A1 and ABA-1B1) showed similar binding affinities for a range of fluorescent active-site probes [retinol, dansylundecanoic acid, dansyl-DL-alpha-amino-octanoic acid, cis-parinaric acid (cPnA)] and for the non-specific hydrophobic surface probe 8-anilinonaphthalene-1-sulphonic acid. However, the molecular environments in the active sites are markedly different, as indicated by disparate fluorescence emission peaks and intensities of bound probes. CD showed that the proteins have similar secondary structures but differ in susceptibility to chemical denaturation/unfolding by guanidinium chloride. Both retain a single conserved tryptophan residue in a characteristic non-polar environment, as revealed by extreme fluorescence blue shift. Thus the gross differences in sequence of the two proteins are not reflected in their ligand-binding specificities but in their binding-site environments.
    Citation
    Moore J, McDermott L, Price NC, Kelly SM, Cooper A, Kennedy MW (1999) 'Sequence-divergent units of the ABA-1 polyprotein array of the nematode Ascaris suum have similar fatty-acid- and retinol-binding properties but different binding-site environments', Biochemical Journal, 340 (), pp.337-343.
    Publisher
    Portland Press
    Journal
    Biochemical Journal
    URI
    http://hdl.handle.net/10547/622680
    DOI
    10.1042/bj3400337
    PubMed ID
    10229690
    Additional Links
    http://www.biochemj.org/content/340/1/337.long
    Type
    Article
    Language
    en
    ISSN
    0264-6021
    ae974a485f413a2113503eed53cd6c53
    10.1042/bj3400337
    Scopus Count
    Collections
    Biomedical and biological science

    entitlement

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