Time-resolved cryo-electron microscopic study of the dissociation of actomyosin induced by photolysis of photolabile nucleotides.
The rapid release of a substrate or other ligand from photolabile precursors in a thin layer suspension of biological specimens followed by rapid freezing provides a method of trapping and visualizing short-lived states in a dynamic system. We demonstrate here the first successful application of this method to study the interaction of actin filaments with myosin subfragment 1 (S1) after release of nucleotides. The results obtained suggest that structural changes in actin filaments occur as a result of interaction with S1.
Ménétret
J F
JF
Max Planck Institute for Medical Research, Department of Biophysics, Heidelberg, Federal Republic of Germany.
Hofmann
W
W
Schröder
R R
RR
Rapp
G
G
Goody
R S
RS
D000199:Actins / Q000648:ultrastructure; D000205:Actomyosin / Q000648:ultrastructure*; D000266:Adenylyl Imidodiphosphate / Q000378:metabolism / Q000494:pharmacology*; D005615:Freezing; D008854:Microscopy, Electron / Q000295:instrumentation / Q000379:methods; D010782:Photolysis
D000199:Actins; D000266:Adenylyl Imidodiphosphate; D000205:Actomyosin