Diversity of Structural Behavior in Vertebrate Conventional Myosins Complexed with Actin

• Published in: Journal of molecular biology 2007-05, Vol.369 (1), p.249-264
• Main Authors: Iwamoto, Hiroyuki, Oiwa, Kazuhiro, Kovács, Mihály, Sellers, James R., Suzuki, Takuya, Wakayama, Jun’ichi, Tamura, Takumi, Yagi, Naoto, Fujisawa, Tetsuro
• Format: Article
• Language: English
• Subjects: Actins - metabolism; Actomyosin - chemistry; Actomyosin - metabolism; actomyosin complex; Adenosine Diphosphate - metabolism; ADP; Animals; Chickens; Crystallography, X-Ray; Kinetics; Models, Molecular; Muscle Fibers, Skeletal - metabolism; myosin subfragment-1; myosin-II; Myosins - chemistry; Myosins - metabolism; Rabbits; Structure-Activity Relationship; Vertebrates - metabolism; X-ray fiber diffraction
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/j.jmb.2007.03.031

Low-resolution three-dimensional structures of acto-myosin subfragment-1 (S1) complexes were retrieved from X-ray fiber diffraction patterns, recorded either in the presence or absence of ADP. The S1 was obtained from various myosin-II isoforms from vertebrates, including rabbit fast-skeletal and cardiac, chicken smooth and human non-muscle IIA and IIB species, and was diffused into an array of overstretched, skinned skeletal muscle fibers. The S1 attached to the exposed actin filaments according to their helical symmetry. Upon addition of ADP, the diffraction patterns from acto–S1 showed an increasing magnitude of response in the order as listed above, with features of a lateral compression of the whole diffraction pattern (indicative of increased radius of the acto–S1 complex) and an enhancement of the fifth layer-line reflection. The structure retrieval indicates that these changes are mainly due to the swing of the light chain (LC) domain in the direction consistent with the cryo-electron microscopic results. In the non-muscle isoforms, the swing is large enough to affect the manner of quasi-crystal packing of the S1-decorated actin filaments and their lattice dimension, with a small change in the twist of actin filaments. Variations also exist in the behavior of the 50K-cleft, which apparently opens upon addition of ADP to the non-muscle isoforms but not to other isoforms. The fast-skeletal S1 remains as the only isoform that does not clearly exhibit either of the structural changes. The results indicate that the “conventional” myosin-II isoforms exhibit a wide variety of structural behavior, possibly depending on their functions and/or the history of molecular evolution.