The Structure of Vertebrate Skeletal-Muscle Myosin Filaments

1982 ◽  
pp. 141-171 ◽  
Author(s):  
Frank A. Pepe
Keyword(s):  
Skeletal Muscle ◽  
Skeletal Muscle Myosin ◽  
Myosin Filaments ◽  
Muscle Myosin ◽  
Vertebrate Skeletal Muscle

scholarly journals Electron microscopy of synthetic myosin filaments. Evidence for cross-bridge. Flexibility and copolymer formation.

1975 ◽  
Vol 67 (1) ◽  
pp. 93-104 ◽  
Author(s):  
T D Pollard
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Structural Features ◽  
Length Frequency ◽  
Single Population ◽  
Skeletal Muscle Myosin ◽  
Distinctive Features ◽  
Myosin Filaments ◽  
The Mean ◽  
Muscle Myosin

Electron micrographs of negatively stained synthetic myosin filaments reveal that surface projections, believed to be the heads of the constituent myosin molecules, can exist in two configurations. Some filaments have the projections disposed close to the filament backbone. Other filaments have all of their projections widely spread, tethered to the backbone by slender threads. Filaments formed from the myosins of skeletal muscle, smooth muscle, and platelets each have distinctive features, particularly their lengths. Soluble mixtures of skeletal muscle myosin with either smooth muscle myosin or platelet myosin were dialyzed against 0.1 M KC1 at pH 7 to determine whether the simultaneous presence of two types of myosin would influence the properties of the filaments formed. In every case, a single population of filaments formed from the mixtures. The resulting filaments are thought to be copolymers of the two types of myosin, for several reasons: (a) their length-frequency distribution is unimodal and differs from that predicted for a simple mixture of two types of myosin filaments; (b) their mean length is intermediate between the mean lengths of the filaments formed separately from the two myosins in the mixture; (c) each of the filaments has structural features characteristic of both of the myosins in the mixture; and (d) their size and shape are determined by the proportion of the two myosins in the mixture.

Calcium sensitivity of vertebrate skeletal muscle myosin

Biochemistry ◽  
1983 ◽  
Vol 22 (10) ◽  
pp. 2324-2331 ◽  
Author(s):  
Dallas L. Pulliam ◽  
Vitaly Sawyna ◽  
Rhea J. C. Levine
Keyword(s):  
Skeletal Muscle ◽  
Calcium Sensitivity ◽  
Skeletal Muscle Myosin ◽  
Muscle Myosin ◽  
Vertebrate Skeletal Muscle

scholarly journals Order-disorder structural transitions in synthetic filaments of fast and slow skeletal muscle myosins under relaxing and activating conditions.

2000 ◽  
Vol 47 (4) ◽  
pp. 1007-1017 ◽  
Author(s):  
Z A Podlubnaya ◽  
S L Malyshev ◽  
K Nieznański ◽  
D Stepkowski
Keyword(s):  
Skeletal Muscle ◽  
Ordered Structure ◽  
Structural Transitions ◽  
Fast Skeletal Muscle ◽  
Skeletal Muscle Myosin ◽  
Slow Skeletal Muscle ◽  
Random Arrangement ◽  
Vertebrate Muscle ◽  
Myosin Filaments ◽  
Muscle Myosin

In the previous study (Podlubnaya et al., 1999, J. Struc. Biol. 127, 1-15) Ca2+-induced reversible structural transitions in synthetic filaments of pure fast skeletal and cardiac muscle myosins were observed under rigor conditions (-Ca2+/+Ca2+). In the present work these studies have been extended to new more order-producing conditions (presence of ATP in the absence of Ca2+) aimed at arresting the relaxed structure in synthetic filaments of both fast and slow skeletal muscle myosin. Filaments were formed from column-purified myosins (rabbit fast skeletal muscle and rabbit slow skeletal semimebranosusproprius muscle). In the presence of 0.1 mM free Ca2+, 3 mM Mg2+ and 2 mM ATP (activating conditions) these filaments had a spread structure with a random arrangement of myosin heads and subfragments 2 protruding from the filament backbone. Such a structure is indistinguishable from the filament structures observed previously for fast skeletal, cardiac (see reference cited above) and smooth (Podlubnaya et al., 1999, J. Muscle Res. Cell Motil. 20, 547-554) muscle myosins in the presence of 0.1 mM free Ca2+. In the absence of Ca2+ and in the presence of ATP (relaxing conditions) the filaments of both studied myosins revealed a compact ordered structure. The fast skeletal muscle myosin filaments exhibited an axial periodicity of about 14.5 nm and which was much more pronounced than under rigor conditions in the absence of Ca2+ (see the first reference cited). The slow skeletal muscle myosin filaments differ slightly in their appearance from those of fast muscle as they exhibit mainly an axial repeat of about 43 nm while the 14.5 nm repeat is visible only in some regions. This may be a result of a slightly different structural properties of slow skeletal muscle myosin. We conclude that, like other filaments of vertebrate myosins, slow skeletal muscle myosin filaments also undergo the Ca2+-induced structural order-disorder transitions. It is very likely that all vertebrate muscle myosins possess such a property.

scholarly journals Force Produced by Smooth and Skeletal Muscle Myosin Filaments Measured with Micro-Fabricated Cantilevers

2018 ◽  
Vol 114 (3) ◽  
pp. 320a
Author(s):  
Yu-Shu Cheng ◽  
Md Rezuanul ◽  
Haque Saikat ◽  
Dilson Rassier
Keyword(s):  
Skeletal Muscle ◽  
Skeletal Muscle Myosin ◽  
Myosin Filaments ◽  
Muscle Myosin

scholarly journals Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase.

1985 ◽  
Vol 260 (20) ◽  
pp. 11275-11285 ◽  
Author(s):  
A M Edelman ◽  
K Takio ◽  
D K Blumenthal ◽  
R S Hansen ◽  
K A Walsh ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Skeletal Muscle Myosin ◽  
Calmodulin Binding ◽  
Catalytic Domains ◽  
Muscle Myosin
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