LC2 involvement in the assembly of skeletal myosin filaments.
The assembly of LC2-deficient myosin was studied under conditions where control and LC2-reassociated myosin assemble around the native length of about 1.5 microns. The aim of this work was to determine how loss of LC2 affects the assembly characteristics. The findings of this study can be summarized as follows: (a) LC2-deficient myosin assembles into two populations of filaments, one around 0.5 micron in length and the other around 1 micron in length. This suggests that loss of the LC2 perturbs the length-determining mechanism. (b) The population of filaments around 0.5 micron has a diameter around 14 nm and that around 1 micron a diameter around 22 nm. Neither diameter corresponds to the 18 nm obtained with the control and LC2-reassociated myosins, suggesting that the presence of LC2 may have a role in regulating the side-to-side assembly of the myosin rods. (c) Filaments assembled from LC2-deficient myosin tend to aggregate side-by-side, but not those assembled from control and LC2-reassociated myosin. (d) The presence of MgATP has no effect on the length distribution of LC2-deficient myosin filaments in contrast to the sharpening of the distribution observed with control and reassociated myosin.
Chowrashi
P K
PK
Department of Anatomy, School of Medicine, University of Pennsylvania, Philadelphia 19104-6058.
Pemrick
S M
SM
Pepe
F A
FA
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D008854:Microscopy, Electron; D009132:Muscles / Q000201:enzymology / Q000648:ultrastructure*; D009218:Myosins / Q000032:analysis* / Q000378:metabolism; D009391:Nephelometry and Turbidimetry; D011108:Polymers; D011817:Rabbits; D013329:Structure-Activity Relationship
D011108:Polymers; D000255:Adenosine Triphosphate; D009218:Myosins