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    DcAGP1, a secreted arabinogalactan protein, is related to a family of basic proline-rich proteins.

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    Authors
    Baldwin, Timothy C.
    Domingo, Concha
    Schindler, Thomas
    Seetharaman, Gouri
    Stacey, Nicola
    Roberts, Keith
    Issue Date
    2001
    
    Metadata
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    Abstract
    A cDNA corresponding to the core protein of an immunoaffinity-purified arabinogalactan protein (AGP) secreted aucus carota (carrot) cells in liquid culture was isolated. This cDNA, DcAGP1, encodes a new class of non-classical' AGP with strong similarity to a family of basic proline-rich proteins. The protein is rich in proline (17%), alanine (10%) and lysine (11%) and contains four distinct domains: a signal peptide, a proline-rich domain, a histidine-rich basic domain and a cysteine-containing 'PAC' domain that is found in a range of other cell wall proteins. The protein contains several sequence motifs found in otherwise unrelated cell wall proteins, but also displays some unique features. Northern blot analyses show that while the DcAGP1 transcript is abundant in the suspension-culture cells from which the AGP was obtained; in carrot seedlings the gene is only expressed at low levels in the roots and it is neither wound- nor stress-inducible. Furthermore, northern and western blot analyses demonstrate that the core polypeptide of DcAGP1 is differentially glycosylated in two different carrot suspension cultures. The unusual features of the protein sequence suggest that the DcAGP1 protein is a member of a family of basic proline-rich proteins defined by the C-terminal PAC domain, and the possible function(s) of the DcAGP1 protein is considered in the light of current views on AGP structure and function.
    Citation
    Plant molecular biology, 45(4): 421-435
    Publisher
    Springer Verlag
    URI
    http://hdl.handle.net/2436/17032
    DOI
    10.1023/A:1010637426934
    PubMed ID
    11352461
    Additional Links
    http://www.springerlink.com/content/t2625751268010wm/
    Type
    Journal article
    Language
    en
    Description
    Metadata only. Full text available at links above.
    ISSN
    0167-4412
    ae974a485f413a2113503eed53cd6c53
    10.1023/A:1010637426934
    Scopus Count
    Collections
    Faculty of Science and Engineering

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