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  • (Tetrahymena)  (2)
  • ATP  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Bioenergetics 1100 (1992), S. 146-154 
    ISSN: 0005-2728
    Schlagwort(e): (Tetrahymena) ; ATPase site ; Dynein, 22S ; Heavy chain ; Thermolysin digestion ; Three heads
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Medizin , Physik
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 2
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 1100 (1992), S. 146-154 
    ISSN: 0167-4838
    Schlagwort(e): (Tetrahymena) ; ATPase site ; Dynein, 22S ; Heavy chain ; Thermolysin digestion ; Three heads
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 3
    Digitale Medien
    Digitale Medien
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 17-25 
    ISSN: 0886-1544
    Schlagwort(e): rotation ; twisting ; microtubule-dynein complex ; 22S dynein ; dynein-track ; ATP ; sliding ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Notizen: Applying a new in vitro motility assay system for microtubules and 22S dynein, we recently reported on an ATP-induced extrusion of microtubules from microtubule-dynein α- and β-complexes [Mimori and Miki-Noumura, 1994:Cell Motil. Cytoskeleton 27:180-191]. In the present study, we prepared a γ-complex by copolymerizing porcine brain tubulin and Tetrahymena ciliary 22S dynein, and examined the ATP-induced microtubule movement from the γ-complex. The extrusion process appeared quite similar to that of the β-complex. The sliding velocity was 18.39 ± 2.20 m̈m/sec, which was a value comparable to that of trypsin-digested flagellar axonemes [Yano and Miki-Noumura, 1980:J. Cell Sci. 44:169-186]. Higher velocity may be due to a densely arranged dynein-track with the same polarity, which was detached from the γ-complex and absorbed in rows on a glass surface of the slide. Sometimes a free-floating microtubule in the perfusion chamber was observed riding and sliding on the dynein-track remaining on the slide after extrusion.Unexpectedly, we found that when the front part of the microtubule was fixed to a glass surface, a continuous sliding microtubule at the rear part on the dyneintrack often transformed into a left-handed helix, and subsequently a twisted helix with several turns. The helix formation may be due to some rigidity in the microtubule and a right-handed torque component in the sliding force of 22S dynein. The addition of ATP may release some distortion accumulated in the complex structure during copolymerization of tubulin and 22S dynein, inducing reverse rotation of the microtubule. © 1995 Wiley-Liss, Inc.
    Zusätzliches Material: 7 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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