In vitro ATP-dependent F-actin sliding on myosin is not influenced by substitution or removal of bound nucleotide.
To examine possible role of F-actin-bound nucleotide in ATP-dependent actin-myosin sliding, we prepared various actin filaments with different nucleotide contents and compared their sliding velocities on heavy mero-myosin in the presence of 2'-deoxyadenosine 5'-triphosphate (dATP) to exclude possible exchange of external ATP with the actin-bound nucleotide. Neither the sliding velocity nor the length of the actin filaments was significantly influenced by substitution or removal of actin-bound nucleotide, indicating that actin-bound nucleotide may not play a significant role in the sliding between actin and myosin.
Oishi
N
N
Radioisotope Research Center, School of Medicine, Teikyo University, Tokyo, Japan.
Sugi
H
H
D000199:Actins / Q000737:chemistry* / Q000302:isolation & purification; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000302:isolation & purification / Q000494:pharmacology*; D000818:Animals; D009119:Muscle Contraction; D009218:Myosins / Q000737:chemistry*; D009711:Nucleotides / Q000032:analysis*; D011817:Rabbits
C022920:ATP-G-actin; D000199:Actins; D009711:Nucleotides; D000255:Adenosine Triphosphate; D009218:Myosins