Binding of actin filaments to connectin.
The binding of actin filaments to connectin, a muscle elastic protein, was investigated by means of turbidity and sedimentation measurements and electron microscopy. In the presence of less than 0.12 M KCl at pH 7.0, actin filaments bound to connectin. Long actin filaments formed bundles. Short actin filaments also aggregated into irregular bundles or a meshwork, and were frequently attached perpendicularly to long bundles. The binding of F-actin to connectin was saturated at an equal weight ratio (molar ratio, 50 : 1), as determined by a cosedimentation assay. Larger amounts of sonicated short actin filaments appeared to bind to connectin than intact F-actin. Myosin S1-decorated actin filaments did not bind to connectin. The addition of S1 to connectin-induced actin bundles resulted in partial disaggregation. Thus, connectin does not appear to interfere with actin-myosin interactions, since myosin S1 binds to actin more strongly than connectin.
Maruyama
K
K
Department of Biology, Faculty of Science, Chiba University.
Hu
D H
DH
Suzuki
T
T
Kimura
S
S
D000199:Actins / Q000378:metabolism*; D000818:Animals; D002645:Chickens; D064211:Connectin; D066298:In Vitro Techniques; D009124:Muscle Proteins / Q000378:metabolism*; D015879:Myosin Subfragments; D009218:Myosins / Q000494:pharmacology; D010446:Peptide Fragments / Q000494:pharmacology; D011189:Potassium Chloride / Q000378:metabolism; D011485:Protein Binding; D011494:Protein Kinases
D000199:Actins; D064211:Connectin; D009124:Muscle Proteins; D015879:Myosin Subfragments; D010446:Peptide Fragments; D011189:Potassium Chloride; D011494:Protein Kinases; D009218:Myosins