Translocation of microtubules caused by the αβ, β and γ outer arm dynein subparticles of <i>Chlamydomonas</i>

DOI PDF 被引用文献8件
  • Hitoshi Sakakibara
    Communications Research Laboratory, 588-2 Iwaoka, Nishi-ku, Kobe 651-24, Japan
  • Haruto Nakayama
    Communications Research Laboratory, 588-2 Iwaoka, Nishi-ku, Kobe 651-24, Japan

抄録

<jats:title>ABSTRACT</jats:title> <jats:p>Three kinds of subparticles of Chlamydomonas outer-arm dynein containing the αβ, β and γ heavy chains were isolated and assayed for their activities to translocate microtubules in vitro. All of them had activities to form bundles of microtubules in solution in an ATP-dependent manner and, when adsorbed on an appropriate glass surface, translocated microtubules. The αβ subparticle readily translocated microtubules on a silicone-coated glass surface with a velocity of 4.6 μm/second at 1 mM ATP. The β subparticle translocated microtubules after it had been preincubated with tubulin dimer and when the Brownian movement of microtubules was suppressed by addition of methylcellulose. The velocity was on average 0.7 μm/second. The γ subparticle translocated microtubules after being preincubated with tubulin dimer and adsorbed onto a silicone-coated glass surface. The velocity was about 3.8 μm/second. The tubulin dimer appeared to facilitate in vitro motility by blocking the ATP-insensitive binding of dynein subparticles to microtubule. The αβ, β and γ subparticles were thus found to have different properties as motor proteins. In addition, these subparticles showed different dependencies upon the potassium acetate concentration. Hence the outer-arm dynein of Chlamydomonas is a complex of motor proteins with different properties.</jats:p>

収録刊行物

被引用文献 (8)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ