Trimethylamine N-oxide suppresses the activity of the actomyosin motor

• Published in: Biochimica et biophysica acta Vol. 1820; no. 10; pp. 1597 - 1604
• Main Authors: Kumemoto, Ryusei, Yusa, Kento, Shibayama, Tomohiro, Hatori, Kuniyuki
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.10.2012
• Subjects: actin; Actin Cytoskeleton - chemistry; Actin Cytoskeleton - drug effects; Actin Cytoskeleton - metabolism; Actomyosin - antagonists & inhibitors; Actomyosin - chemistry; Actomyosin - metabolism; Adenosine Triphosphatases - metabolism; adenosine triphosphate; adenosinetriphosphatase; Animals; ATP hydrolysis; ATPase; circular dichroism spectroscopy; Dose-Response Relationship, Drug; Down-Regulation - drug effects; energy; fluorescence; heavy meromyosin; Hydration; hydrogen bonding; hydrolysis; In Vitro Techniques; malachite green; Methylamines - pharmacology; microfilaments; Motility; Movement - drug effects; Multiprotein Complexes - chemistry; Multiprotein Complexes - metabolism; Muscular protein; Myosin Subfragments - chemistry; Myosin Subfragments - metabolism; Osmolar Concentration; Osmolyte; Protein Stability - drug effects; Rabbits; skeletal muscle; trimethylamine; Urea; Urea - pharmacology; water stress; TMAO; Motility; ATP hydrolysis; Hydration; HMM; Muscular protein; PCA; BSA; Urea; Pi; bis-ANS; Osmolyte; ATP

During actomyosin interactions, the transduction of energy from ATP hydrolysis to motility seems to occur with the modulation of hydration. Trimethylamine N-oxide (TMAO) perturbs the surface of proteins by altering hydrogen bonding in a manner opposite to that of urea. Hence, we focus on the effects...