Assignment of the human fast skeletal muscle myosin alkali light chains gene (MLC1F/MLC3F) to 2q 32.1-2qter

1988 ◽  
Vol 78 (1) ◽  
pp. 65-70 ◽  
Author(s):  
Odile Cohen-Haguenauer ◽  
Paul J. R. Barton ◽  
Nguyen Van Cong ◽  
Stéphane Serero ◽  
Marie-Sylvie Gross ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Light Chains ◽  
Fast Skeletal Muscle ◽  
Skeletal Muscle Myosin ◽  
Muscle Myosin

scholarly journals Structure and function of fish fast skeletal muscle myosin light chains

2002 ◽  
Vol 68 (sup2) ◽  
pp. 1499-1502 ◽  
Author(s):  
SHOICHIRO ISHIZAKI ◽  
YASUYUKI MASUDA ◽  
MUNEHIKO TANAKA ◽  
SHUGO WATABE
Keyword(s):  
Skeletal Muscle ◽  
Structure And Function ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Fast Skeletal Muscle ◽  
Skeletal Muscle Myosin ◽  
And Function ◽  
Muscle Myosin

scholarly journals Properties of the non-specific calcium-binding sites of rabbit skeletal-muscle myosin

1980 ◽  
Vol 185 (1) ◽  
pp. 265-268 ◽  
Author(s):  
J Wikman-Coffelt
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Binding Sites ◽  
Calcium Binding ◽  
Light Chains ◽  
Binding Properties ◽  
Skeletal Muscle Myosin ◽  
Heavy Chains ◽  
Calcium Binding Sites ◽  
Muscle Myosin

The non-specific Ca2+-binding sites of skeletal-muscle myosin are located on the light chains; with the dissociation of light chains there is a corresponding decrease in the number of Ca2+-binding sites on light-chain-deficient myosin. The released light chains have a decreased binding affinity. Myosin heavy chains indirectly influence the Ca2+-binding properties of light chains by increasing the affinity of light chains for bivalent cations; this influence varies with pH. Because of light-chain dissociation at low Ca2+ and/or Mg2+ concentrations, anomalies may exist when analyses of non-specific Ca2+-binding properties of myosin are assessed by dialysis equilibrium.

scholarly journals Regulatory Light Chains Fine-Tune Skeletal Muscle Myosin-II Function

2021 ◽  
Vol 120 (3) ◽  
pp. 344a
Author(s):  
Arnab Nayak ◽  
Tianbang Wang ◽  
Peter Franz ◽  
Walter Steffen ◽  
Igor Chizhov ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Ii ◽  
Light Chains ◽  
Skeletal Muscle Myosin ◽  
Regulatory Light Chains ◽  
Muscle Myosin ◽  
Fine Tune

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.

Skeletal muscle myosin light chains are essential for physiological speeds of shortening

Nature ◽  
1993 ◽  
Vol 365 (6445) ◽  
pp. 454-456 ◽  
Author(s):  
Susan Lowey ◽  
Guillermina S. Waller ◽  
Kathleen M. Trybus
Keyword(s):  
Skeletal Muscle ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Skeletal Muscle Myosin ◽  
Muscle Myosin
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