scholarly journals Interaction of isolated cross‐linked short actin oligomers with the skeletal muscle myosin motor domain

FEBS Journal ◽  
2018 ◽  
Vol 285 (9) ◽  
pp. 1715-1729 ◽  
Author(s):  
Zheng Qu ◽  
Setsuko Fujita‐Becker ◽  
Edda Ballweber ◽  
Semra Ince ◽  
Christian Herrmann ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Motor Domain ◽  
Skeletal Muscle Myosin ◽  
Myosin Motor ◽  
Myosin Motor Domain ◽  
Muscle Myosin

scholarly journals The structure of the actin-smooth muscle myosin motor domain complex in the rigor state

2017 ◽  
Vol 200 (3) ◽  
pp. 325-333 ◽  
Author(s):  
Chaity Banerjee ◽  
Zhongjun Hu ◽  
Zhong Huang ◽  
J. Anthony Warrington ◽  
Dianne W. Taylor ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Myosin ◽  
Motor Domain ◽  
Myosin Motor ◽  
Rigor State ◽  
Myosin Motor Domain ◽  
Muscle Myosin

scholarly journals Folding of the Striated Muscle Myosin Motor Domain

2002 ◽  
Vol 277 (39) ◽  
pp. 36799-36807 ◽  
Author(s):  
Diana Chow ◽  
Rajani Srikakulam ◽  
Ying Chen ◽  
Donald A. Winkelmann
Keyword(s):  
Striated Muscle ◽  
Motor Domain ◽  
Myosin Motor ◽  
Myosin Motor Domain ◽  
Muscle Myosin

scholarly journals A Minimal Motor Domain from Chicken Skeletal Muscle Myosin

1995 ◽  
Vol 270 (25) ◽  
pp. 15348-15352 ◽  
Author(s):  
Guillermina S. Waller ◽  
Greta Ouyang ◽  
James Swafford ◽  
Peter Vibert ◽  
Susan Lowey
Keyword(s):  
Skeletal Muscle ◽  
Motor Domain ◽  
Skeletal Muscle Myosin ◽  
Muscle Myosin ◽  
Chicken Skeletal Muscle

scholarly journals Glycine 699 is pivotal for the motor activity of skeletal muscle myosin.

1996 ◽  
Vol 134 (4) ◽  
pp. 895-909 ◽  
Author(s):  
F Kinose ◽  
S X Wang ◽  
U S Kidambi ◽  
C L Moncman ◽  
D A Winkelmann
Keyword(s):  
Skeletal Muscle ◽  
Motor Activity ◽  
Expression System ◽  
Motor Domain ◽  
C2c12 Cells ◽  
Myosin Isoforms ◽  
Skeletal Muscle Myosin ◽  
Lever Arm ◽  
Wide Range ◽  
Muscle Myosin

Myosin couples ATP hydrolysis to the translocation of actin filaments to power many forms of cellular motility. A striking feature of the structure of the muscle myosin head domain is a 9-nm long "lever arm" that has been postulated to produce a 5-10-nm power stroke. This motion must be coupled to conformational changes around the actin and nucleotide binding sites. The linkage of these sites to the lever arm has been analyzed by site-directed mutagenesis of a conserved glycine residue (G699) found in a bend joining two helices containing the highly reactive and mobile cysteine residues, SH1 and SH2. Alanine mutagenesis of this glycine (G699A) dramatically alters the motor activity of skeletal muscle myosin, inhibiting the velocity of actin filament movement by > 100-fold. Analysis of the defect in the G699A mutant myosin is consistent with a marked slowing of the transition within the motor domain from a strong binding to a weak binding interaction with actin. This result is interpreted in terms of the role of this residue (G699) as a pivot point for motion of the lever arm. The recombinant myosin used in these experiments has been produced in a unique expression system. A shuttle vector containing a regulated muscle-specific promoter has been developed for the stable expression of recombinant myosin in C2C12 cells. The vector uses the promoter/enhancer region, the first two and the last five exons of an embryonic rat myosin gene, to regulate the expression of an embryonic chicken muscle myosin cDNA. Stable cell lines transfected with this vector express the unique genetically engineered myosin after differentiation into myotubes. The myosin assembles into myofibrils, copurifies with the endogenous myosin, and contains a complement of muscle-specific myosin light chains. The functional activity of the recombinant myosin is readily analyzed with an in vitro motility assay using a species-specific anti-S2 mAb to selectively assay the recombinant protein. This expression system has facilitated manipulation and analysis of the skeletal muscle myosin motor domain and is also amenable to a wide range of structure-function experiments addressing questions unique to the muscle-specific cytoarchitecture and myosin isoforms.

Stimulatory effects of arachidonic acid on myosin ATPase activity and contraction of smooth muscle via myosin motor domain

2010 ◽  
Vol 298 (2) ◽  
pp. H505-H514 ◽  
Author(s):  
Takeshi Katayama ◽  
Masaru Watanabe ◽  
Hideyuki Tanaka ◽  
Mizuki Hino ◽  
Takuya Miyakawa ◽  
...  
Keyword(s):  
Arachidonic Acid ◽  
Smooth Muscle ◽  
Atpase Activity ◽  
Smooth Muscle Myosin ◽  
Motor Domain ◽  
Actin Binding ◽  
Smooth Muscle Tissue ◽  
Myosin Motor ◽  
Myosin Motor Domain ◽  
Muscle Myosin

We have been searching for a mechanism to induce smooth muscle contraction that is not associated with phosphorylation of the regulatory light chain (RLC) of smooth muscle myosin (Nakamura A, Xie C, Zhang Y, Gao Y, Wang HH, Ye LH, Kishi H, Okagaki T, Yoshiyama S, Hayakawa K, Ishikawa R, Kohama K. Biochem Biophys Res Commun 369: 135–143, 2008). In this article, we report that arachidonic acid (AA) stimulates ATPase activity of unphosphorylated smooth muscle myosin with maximal stimulation (Rmax) of 6.84 ± 0.51 relative to stimulation by the vehicle and with a half-maximal effective concentration (EC50) of 50.3 ± 4.2 μM. In the presence of actin, Rmax was 1.72 ± 0.08 and EC50 was 26.3 ± 2.3 μM. Our experiments with eicosanoids consisting of the AA cascade suggested that they neither stimulated nor inhibited the activity. Under conditions that did not allow RLC to be phosphorylated, AA stimulated contraction of smooth muscle tissue with an Rmax of 1.45 ± 0.07 and an EC50 of 27.0 ± 4.4 μM. In addition to the ATPase activities of the myosin, AA stimulated those of heavy meromyosin, subfragment 1 (S1), S1 from which the RLC was removed, and a recombinant heavy chain consisting of the myosin head. The stimulatory effects of AA on these preparations were about twofold. The site of AA action was indicated to be the step-releasing inorganic phosphate (Pi) from the reaction intermediate of the myosin-ADP-Pi complex. The enhancement of Pi release by AA was supported by computer simulation indicating that AA docked in the actin-binding cleft of the myosin motor domain. The stimulatory effect of AA was detectable with both unphosphorylated myosin and the myosin in which RLC was fully phosphorylated. The AA effect on both myosin forms was suggested to cause excess contraction such as vasospasm.

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