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  • 1
    Electronic Resource
    Electronic Resource
    The 135-kDa actin-bundling protein from lily pollen tubes arranges F-actin into bundles with uniform polarity (1999)
    Springer
    Planta 209 (1999), S. 264-266 
    Details
    ISSN: 1432-2048
    Keywords: Key words: Actin ; Actin bundling protein ; Lilium (pollen tube) ; Pollen tube
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract.  A plant 135-kDa actin-bundling protein (P-135-ABP) isolated from pollen tubes of Lilium longiflorum (Thunb.) binds stoichiometrically to F-actin filaments and bundles them in vitro (E. Yokota et al., 1998, Plant Physiol. 116: 1421–1429). To further understand the mechanism of actin-filament bundle formation by P-135-ABP, the polarity of each F-actin filament in bundles was examined using myosin subfragment 1 (S-1). Dissociation of F-actin filaments from bundles organized by P-135-ABP was induced by S-1. However, F-actin filaments that remained in a bundle and decorated by S-1 showed uniform polarity. These results indicate that P-135-ABP arranges F-actin filaments into bundles with uniform polarity and consequently plays a key role in the orientation of cytoplasmic streaming in pollen tubes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050631
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  • 2
    Electronic Resource
    Electronic Resource
    The outer arm dynein α-heavy chains of sea urchin sperm flagella and embryonic cilia are different (1990)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 16 (1990), S. 58-67 
    Details
    ISSN: 0886-1544
    Keywords: subunit composition ; Western blotting ; monoclonal antibody ; affinity-purified polyclonal antibody ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Sea urchin sperm outer arm dynein is a multi-subunit protein composed of heavy chains, intermediate chains, and light chains. We prepared monoclonal and affinity-purified polyclonal antibodies to heavy and intermediate chain subunits and examined whether the embryonic ciliary axonemes ofthe same species contain the polypeptides sharing epitopes with them. Ciliary axonemes contained a high molecular weight polypeptide with the exact same mobility as flagellar β-heavy chain. This polypeptide also shared epitopes with it. In contrast, no polypeptide had the exact same molecular weight as flagellar α-heavy chain and shared epitopes with it. Western blots showed that ciliary axonemes also contain three polypeptides sharing epitopes with the respective flagellar intermediate chain. The present results revealed that the α-heavy chains of flagellar and ciliary outer arm dyneins are different.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970160108
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