Electron microscopic observation of monomeric actin attached to a myosin head.
Attachment of G-actin to a myosin head was for the first time visualized by electron microscopy of heavy meromyosin (HMM) molecules decorated using a chemical crosslinker with G-actin, which is made resistant to salt- and myosin-induced polymerization by treatment with m-maleimidobenzoic acid N-hydroxysuccinimide ester (MBS). Rotary-shadowed images of acto-HMM molecules crosslinked using MBS or water-soluble carbodiimide showed that MBS-G-actin binds to the distal half of a myosin head (the region 14-15 nm away from the head-rod junction).
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Graduate School of Science, Osaka University, Machikaneyama 1-1, Osaka, Toyonaka, 560-0043, Japan.
D000199:Actins / Q000648:ultrastructure*; D000818:Animals; D001665:Binding Sites / Q000502:physiology; D003432:Cross-Linking Reagents / Q000378:metabolism; D005022:Ethyldimethylaminopropyl Carbodiimide / Q000031:analogs & derivatives / Q000378:metabolism; D008854:Microscopy, Electron; D009124:Muscle Proteins / Q000648:ultrastructure; D015879:Myosin Subfragments / Q000648:ultrastructure; D009218:Myosins / Q000648:ultrastructure*; D011485:Protein Binding / Q000502:physiology; D011817:Rabbits; D013388:Succinimides / Q000378:metabolism
D000199:Actins; D003432:Cross-Linking Reagents; D009124:Muscle Proteins; D015879:Myosin Subfragments; D013388:Succinimides; C066969:maleimidobenzoyl-G-actin; C013097:3-maleimidobenzoyl N-hydroxysuccinimide; C041829:1-ethyl-3-(3-(dimethylamino)propyl)carbodiimide methiodide; D009218:Myosins; D005022:Ethyldimethylaminopropyl Carbodiimide