Orientation of actin monomer in the F-actin filament: radial coordinate of glutamine-41 and effect of myosin subfragment 1 binding on the monomer orientation [Erratum to document cited in CA109(1):2635d]

Biochemistry ◽  
1988 ◽  
Vol 27 (22) ◽  
pp. 8508-8508
Author(s):  
Andrzej A. Kasprzak ◽  
Reiji Takashi ◽  
Manuel F. Morales
Keyword(s):  
Actin Filament ◽  
Radial Coordinate ◽  
Actin Monomer ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1

Potentiated state of the tropomyosin actin filament and nucleotide-containing myosin subfragment 1

Biochemistry ◽  
1982 ◽  
Vol 21 (5) ◽  
pp. 906-915 ◽  
Author(s):  
John M. Murray ◽  
Mary K. Knox ◽  
Cynthia E. Trueblood ◽  
Annemarie Weber
Keyword(s):  
Actin Filament ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1

scholarly journals The visualization of actin filament polarity in thin sections. Evidence for the uniform polarity of membrane-associated filaments.

1978 ◽  
Vol 79 (3) ◽  
pp. 846-852 ◽  
Author(s):  
D A Begg ◽  
R Rodewald ◽  
L I Rebhun
Keyword(s):  
Actin Filament ◽  
Actin Filaments ◽  
Intestinal Epithelial ◽  
Improved Method ◽  
Thin Sections ◽  
Myosin Subfragment ◽  
Brush Borders ◽  
Nonmuscle Cells ◽  
Myosin Subfragment 1 ◽  
Uniform Polarity

We have developed an improved method for visualizing actin filament polarity in thin sections. Myosin subfragment-1 (S-1)-decorated actin filaments display a dramatically enhanced arrowhead configuration when fixed in a medium which contains 0.2 % tannic acid. With the exception of brush borders from intestinal epithelial cells, the arrowhead periodicity of decorated filaments in a variety of nonmuscle cells is similar to that in isolated myofibrils. The periodicity of decorated filaments in brush borders is significantly smaller. Actin filaments which attach to membranes display a clear, uniform polarity, with the S-1 arrowheads pointing away from the plasma membrane, while those which comprise the stress fibers of myoblasts and CHO cells have antiparallel polarities. These observations are consistent with a sliding filament mechanism of cell motility.

scholarly journals Identification of actin filaments in the rhabdomeral microvilli of Drosophila photoreceptors.

1990 ◽  
Vol 110 (6) ◽  
pp. 1993-1998 ◽  
Author(s):  
K Arikawa ◽  
J L Hicks ◽  
D S Williams
Keyword(s):  
Actin Filament ◽  
Brush Border ◽  
Actin Filaments ◽  
Immunogold Labeling ◽  
Entire Length ◽  
Filamentous Actin ◽  
Fast Growing ◽  
Intestinal Brush Border ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1

The phototransductive microvilli of arthropod photoreceptors each contain an axial cytoskeleton. The present study shows that actin filaments are a component of this cytoskeleton in Drosophila. Firstly, actin was detected in the rhabdomeral microvilli and in the subrhabdomeral cytoplasm by immunogold labeling with antiactin. Secondly, the rhabdomeres were labeled with phalloidin, indicating the presence of filamentous actin. Finally, the actin filaments were decorated with myosin subfragment-1. The characteristic arrowhead complex formed by subfragment-1 decoration points towards the base of the microvilli, so that the fast growing end of each filament is at the distal end of the microvillus, where it is embedded in a detergent-resistant cap. Each microvillus contains more than one actin filament. Decorated filaments extend the entire length of each microvillus and project into the subrhabdomeral cytoplasm. This organization is comparable to that of the actin filaments in intestinal brush border microvilli. Similar observations were made with the photoreceptor microvilli of the crayfish, Procambarus. Our results provide an indication as to how any myosin that is associated with the rhabdomeres might function.

scholarly journals Polymerization of actin. VI. The polarity of the actin filaments in the acrosomal process and how it might be determined.

1979 ◽  
Vol 81 (3) ◽  
pp. 608-623 ◽  
Author(s):  
L G Tilney ◽  
N Kallenbach
Keyword(s):  
Low Temperature ◽  
Actin Filaments ◽  
Critical Concentration ◽  
Actin Monomer ◽  
Spontaneous Nucleation ◽  
Myosin Subfragment ◽  
Acrosomal Reaction ◽  
Myosin Subfragment 1

The polarity of the actin filaments which assemble from the nucleating body or actomere of Thyone and Pisaster sperm was determined using myosin subfragment 1 decoration. The polarity was found to be unidirectional with the arrowheads pointing towards the cell center. When polymerization is induced at low temperature with concentrations of actin near the critical concentration for polymerization, elongation of filaments occurs preferentially off the apical end. If the sperm are induced to undergo the acrosomal reaction with an ionophore, the polarity of the actin filaments attached to the actomere is the same as that already described, but the filaments which polymerize parallel to, but peripheral to, those extending from the actomere are randomly polarized. These randomly polarized filaments appear to result from spontaneous nucleation. When sperm are induced to undergo the acrosomal reaction with eggs, the polarity of the actin filaments is also unidirectional with the arrowheads pointing towards the cell center. From these results we conclude: (a) that the actomere, by nucleating the polymerization of actin filaments, controls the polarity of the actin filaments in the acrosomal process, (b) that the actomere recognizes a surface of the actin monomer that is different from that surface recognized by the dense material attached to membranes, and (c) that egg myosin could not act to pull the sperm into the egg. Included is a discussion of how the observation that monomers add largely to one end of a decorated filament in vitro relates to these in vivo observations.

Structure of Myosin Subfragment-1 from Electron Microscopy and Crystallography

1988 ◽  
Vol 46 ◽  
pp. 156-157
Author(s):  
Donald A. Winkelmann
Keyword(s):  
Electron Microscopy ◽  
Molecular Weight ◽  
Actin Filaments ◽  
Light Chains ◽  
Myosin Filament ◽  
Primary Role ◽  
Heavy Chains ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Globular Head

The primary role of the interaction of actin and myosin is the generation of force and motion as a direct consequence of the cyclic interaction of myosin crossbridges with actin filaments. Myosin is composed of six polypeptides: two heavy chains of molecular weight 220,000 daltons and two pairs of light chains of molecular weight 17,000-23,000. The C-terminal portions of the myosin heavy chains associate to form an α-helical coiled-coil rod which is responsible for myosin filament formation. The N-terminal portion of each heavy chain associates with two different light chains to form a globular head that binds actin and hydrolyses ATP. Myosin can be fragmented by limited proteolysis into several structural and functional domains. It has recently been demonstrated using an in vitro movement assay that the globular head domain, subfragment-1, is sufficient to cause sliding movement of actin filaments.The discovery of conditions for crystallization of the myosin subfragment-1 (S1) has led to a systematic analysis of S1 structure by x-ray crystallography and electron microscopy. Image analysis of electron micrographs of thin sections of small S1 crystals has been used to determine the structure of S1 in the crystal lattice.

scholarly journals Studies of Ligand-induced Conformational Perturbations in Myosin Subfragment 1

1989 ◽  
Vol 264 (18) ◽  
pp. 10810-10819
Author(s):  
K N Rajasekharan ◽  
M Mayadevi ◽  
M Burke
Keyword(s):  
Myosin Subfragment ◽  
Myosin Subfragment 1
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