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Association of a Myosin Motor with Membrane-Bounded Pigment Granules in Freshwater Shrimp Chromatophores: Evidence from the Nitella Actin-Cable Assay

Association of a Myosin Motor with Membrane-Bounded Pigment Granules in Freshwater Shrimp... We have adapted an actin-myosin motility assay to examine the interactions in vitro between actin cables isolated from the giant internodal cells of the freshwater alga, Nitella , and pigment granules extracted from red ovarian chromatophores of the freshwater palaemonid shrimp, Macrobrachium olfersi . The chromatophore pigment mass consists of large (0.5–1.0-µm diameter) membrane-bounded granules, and small (140-nm diameter), amembranous granules, both structurally continuous with the abundant smooth endoplasmic reticulum. Our previous immunocytochemical studies show a myosin motor to be stably associated with the pigment mass; however, to which granule type or membrane the myosin motor is attached is unclear. Here, we show that sodium vanadate, a myosin ATPase inhibitor, markedly increases the affinity of isolated, large, membrane-bounded granules for Nitella actin cables to which they become permanently attached. This interaction does not occur in granule preparations containing ATP with uninhibited, active myosin without vanadate. We propose that a stable state of elevated affinity is established between the granule-located myosin motor and the Nitella actin cables, resulting from a vanadate-inhibited acto-myosin-ADP complex. This finding provides further evidence for a myosin motor positioned on the surface of the membrane-bounded pigment granules in shrimp ovarian chromatophores. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Crustacean Biology Brill

Association of a Myosin Motor with Membrane-Bounded Pigment Granules in Freshwater Shrimp Chromatophores: Evidence from the Nitella Actin-Cable Assay

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References (44)

Publisher
Brill
Copyright
The Crustacean Society
Subject
Physiology
ISSN
0278-0372
eISSN
1937-240X
DOI
10.1651/08-3086.1
Publisher site
See Article on Publisher Site

Abstract

We have adapted an actin-myosin motility assay to examine the interactions in vitro between actin cables isolated from the giant internodal cells of the freshwater alga, Nitella , and pigment granules extracted from red ovarian chromatophores of the freshwater palaemonid shrimp, Macrobrachium olfersi . The chromatophore pigment mass consists of large (0.5–1.0-µm diameter) membrane-bounded granules, and small (140-nm diameter), amembranous granules, both structurally continuous with the abundant smooth endoplasmic reticulum. Our previous immunocytochemical studies show a myosin motor to be stably associated with the pigment mass; however, to which granule type or membrane the myosin motor is attached is unclear. Here, we show that sodium vanadate, a myosin ATPase inhibitor, markedly increases the affinity of isolated, large, membrane-bounded granules for Nitella actin cables to which they become permanently attached. This interaction does not occur in granule preparations containing ATP with uninhibited, active myosin without vanadate. We propose that a stable state of elevated affinity is established between the granule-located myosin motor and the Nitella actin cables, resulting from a vanadate-inhibited acto-myosin-ADP complex. This finding provides further evidence for a myosin motor positioned on the surface of the membrane-bounded pigment granules in shrimp ovarian chromatophores.

Journal

Journal of Crustacean BiologyBrill

Published: Aug 1, 2009

Keywords: actin; chromatic adaptation; myosin ATPase; pigment granule translocation; vanadate inhibition

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