Literature DB >> 8956480

Mutual sensitization of ATP and GTP in driving F-actin on the surface-fixed H-meromyosin.

T Oda1, Y Shikata, K Mihashi.   

Abstract

Using an in vitro motility assay on acto-H-meromyosin, we studied the sliding velocity of an actin filament driven by two kinds of H-meromyosin heads: H-meromyosin head with ATP bound (fast motor) and with GTP bound (slow motor). We found a significant increase in the sliding velocity owing to the coexistence of the fast motor and the slow motor. This phenomenon may give an important suggestion with regard to the integration over multiple interactions of H-meromyosin heads along the actin filament.

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Year:  1996        PMID: 8956480     DOI: 10.1016/s0301-4622(96)00023-3

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  2 in total

1.  Longitudinal distortions and transversal fluctuations of an actin filament sliding on Myosin molecules.

Authors:  H Honda; K Kikuchi; K Hatori; E Imai; K Shimada; K Matsuno
Journal:  J Biol Phys       Date:  2002-09       Impact factor: 1.365

2.  Acceleration of the sliding movement of actin filaments with the use of a non-motile mutant myosin in in vitro motility assays driven by skeletal muscle heavy meromyosin.

Authors:  Kohei Iwase; Masateru Tanaka; Keiko Hirose; Taro Q P Uyeda; Hajime Honda
Journal:  PLoS One       Date:  2017-07-24       Impact factor: 3.240

  2 in total

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