N-Terminus of Cardiac Myosin Essential Light Chain Modulates Myosin Step-Size
نویسندگان
چکیده
منابع مشابه
Myosin light-chain kinase of smooth muscle stimulates myosin ATPase activity without phosphorylating myosin light chain.
Myosin light-chain kinase (MLCK) of smooth muscle is multifunctional, being composed of N-terminal actin-binding domain, central kinase domain, and C-terminal myosin-binding domain. The kinase domain is the best characterized; this domain activates the interaction of smooth-muscle myosin with actin by phosphorylating the myosin light chain. We have recently shown that the Met-1-Pro-41 sequence ...
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We compared the thermal aggregation properties of two isoforms of the isolated myosin head (myosin subfragment 1, S1) containing different "essential" (or "alkali") light chains, A1 or A2. Temperature dependencies for the aggregation of these two S1 isoforms, as measured by the increase in turbidity, were compared with the temperature dependencies of their thermal denaturation obtained from dif...
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AIMS We tested the hypothesis that mutations in the human ventricular essential myosin light chain (hVLC-1) that are associated with hypertrophic cardiomyopathy (HCM) affect protein structure, binding to the IQ1 motif of cardiac myosin heavy chain (MYH) and sarcomeric sorting in neonatal cardiomyocytes. METHODS AND RESULTS We employed circular dichroism and surface plasmon resonance spectrosc...
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The essential light chain of myosin (ELC) is known to be important for structural stability of the alpha-helical lever arm domain of the myosin head, but its function in striated muscle contraction is poorly understood. Two ELC isoforms are expressed in fast skeletal muscle, a long isoform and its NH(2)-terminal approximately 40 amino acid shorter counterpart, whereas only the long ELC is obser...
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ژورنال
عنوان ژورنال: Biochemistry
سال: 2015
ISSN: 0006-2960,1520-4995
DOI: 10.1021/acs.biochem.5b00817