Abstract
In the streaming cytoplasm of the Characean algae cell, the movement of organelles along actin bundles occurs at a striking rate of up to 60 μm s-1. To further characterize the molecular mechanisms responsible for this phenomenon, we have reconstituted the movement of actin filaments in vitro using defined biochemical components. We report that only a soluble cytoplasmic fraction devoid of organelles and filamentous material supports the movement of fluorescent-labeled actin filaments on glass at a rate of up to 60 μm s-1. This fraction also contains the K+-EDTA ATPase and the actin-activated Mg2+ ATPase activities characteristic of myosin proteins. Therefore, on the basis of these observations, we conclude that Nitella cells have a soluble pool of non-filamentous myosin molecules with the mechanochemical properties expected for a motor responsible for cytoplasmic streaming in vivo. The preparation and conditions described here should be useful for the purification of this translocator.
Original language | English (US) |
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Pages (from-to) | 1-4 |
Number of pages | 4 |
Journal | BBA - Bioenergetics |
Volume | 1232 |
Issue number | 1-2 |
DOIs | |
State | Published - Nov 21 1995 |
Keywords
- Actin
- Motility
- Myosin
- Video microscopy
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Cell Biology