Paratnyosin paracrystails formned with divalent cations have a 725-angstrom axial period and show simple negative staining patterns in the electron microscope. The structure of the aggregates is interpreted in terms of an array of polar molecules about 1275 angstroms long, with "gaps" and "overlaps" in the molecular assembly. Antiparallel relatiotns between molecules lead to the assembly of paracrystals with opposite polarity at either end. Implications of the in vitro structure for filaments containing paramyosin in muscle are discussed.

Animals↗

PubMed1967

Protein synthesis and enzyme response to contractile activity in skeletal muscle.

Explore the source record for details and available documents.

Alanine↗

PubMed1967

The enzymes of adenine nucleotide metabolism in developing skeletal muscle.

1. During late foetal and early post-natal development of rabbit skeletal muscle the total protein increased more rapidly than the non-protein nitrogen content per g. wet wt. 2. AMP-deaminase activity of rabbit leg muscles increased rapidly over the period 5-15 days after birth. In diaphragm muscle from the same animal the rapid increase to the adult enzymic activity took place at about the time of birth. 3. The rapid increase in AMP-deaminase activity of leg muscle occurred earlier in animals born relatively mature, such as the chick and guinea pig, than in animals less well developed at birth, such as the rabbit and rat. 4. The pattern of enzymic activity shown by AMP deaminase during development in diaphragm, leg and cardiac muscles in a given species was closely paralleled by those of adenylate kinase and creatine phosphokinase. 5. When young rabbits were encouraged to become active at an earlier stage than is normal, the rise in creatine-phosphokinase activity occurred at an earlier age than in the control animals. 6. The results suggest that the activity pattern of the muscle is an important factor in determining the time at which the activities of the enzymes of special significance for muscle rise sharply to the adult values. 7. Development in rabbit leg muscle also involved an increase in aldolase activity. The pattern of change was similar to that obtained with other enzymes studied.

Adenine Nucleotides↗

PubMed1965

Enzymatic adaptation to contractile activity in skeletal muscle.

Explore the source record for details and available documents.

Animals↗

PubMedDate not supplied

Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules.

Phosphorylation of the 20,000-molecular weight (Mr) light chains of vertebrate non-muscle (thymus) and smooth muscle (gizzard) myosins regulates the assembly of these myosins into filaments in vitro. At physiological ionic strength and pH, nonphosphorylated smooth muscle and non-muscle myosin filaments are disassembled by stoichiometric levels of MgATP, forming species having sedimentation coefficients of approximately 11S (range 10-12S; myosin monomers in high salt sediment at 6S). When the 20,000 (20K)-Mr light chains on these 11S myosin species are phosphorylated by the light-chain kinase/calmodulin-Ca2+ complex, the inhibitory effect of the light chains on filament formation is removed and the myosins reassemble into filaments which are stable in MgATP. It was originally suggested that the 11S myosin species was a dimer, previously suggested as a building block for smooth muscle and non-muscle myosin filaments. It has since been shown, however, that 11S smooth muscle myosin is monomeric and has a folded conformation rather than the extended shape characteristic of monomeric myosin in high salt. Here we show that 11S non-muscle myosin is also folded and that phosphorylation of the 20K-Mr light chains of both vertebrate non-muscle (thymus) and vertebrate smooth muscle (gizzard) myosins causes these folded 11S molecules to unfold into the conventional extended monomeric form, which is able to assemble into filaments.

Animals↗

PubMedDate not supplied

Site-directed mutagenesis of the regulatory light-chain Ca2+/Mg2+ binding site and its role in hybrid myosins.

The regulatory light chains, small polypeptides located on the myosin head, regulate the interaction of myosin with actin in response to either Ca2+ or phosphorylation. The demonstration that the regulatory light chains on scallop myosin can be replaced by light chains from other myosins has allowed us to compare the functional capabilities of different light chains, but has not enabled us to probe the role of features, such as the Ca2+/Mg2+ binding site, that are common to all of them. Here, we describe the use of site-directed mutagenesis to study the function of that site. We synthesized the chicken skeletal myosin light chain in Escherichia coli and constructed mutants with substitutions within the Ca2+/Mg2+ binding site. When the aspartate residues at the first and sixth Ca2+ coordination positions are replaced by uncharged alanines, the light chains have a reduced Ca2+ binding capacity but still bind to scallop myosin with high affinity. Unlike the wild-type skeletal light chain which inhibits myosin interaction with actin, the mutants activate it. Thus, an intact Ca2+/Mg2+ binding site in the N-terminal region of the light chain is essential for regulating the interaction of myosin with actin.

Actins↗