[N-ethylmaleimide inhibits polymerization of myorod, a contractile protein of thick filaments of molluscan smooth muscles].
The effect of N-ethylmaleimide on the polymerization of myorod, a protein of molluscan smooth muscles, which is colocalized with myosin on the surface of paramyosin core of thick filaments and is a product of the alternative splicing of the gene of heavy myosin chains, was studied. It was shown that myorod modified by N-ethylmaleimide completely loses the polymerization ability but acquires the ability to aggregate in the presence of Mg2+. At the same time, treatment of molluscan myosin with N-ethylmaleimide did not affect its polymerization. It was supposed that the effect of N-ethylmaleimide on myorod polymerization is related to the modification of the myorod SH domain containing Cys722.
Matusovskaia
G G
GG
Permiakova
T V
TV
Matusovskiĭ
O S
OS
Shelud'ko
N S
NS
D008841:Actin Cytoskeleton / Q000378:metabolism; D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D001704:Biopolymers / Q000737:chemistry*; D003285:Contractile Proteins / Q000737:chemistry*; D003545:Cysteine / Q000737:chemistry; D005033:Ethylmaleimide / Q000737:chemistry*; D008274:Magnesium / Q000737:chemistry; D008969:Molecular Sequence Data; D008974:Mollusca / Q000378:metabolism*; D009130:Muscle, Smooth / Q000378:metabolism*; D009218:Myosins / Q000737:chemistry
D001704:Biopolymers; D003285:Contractile Proteins; D009218:Myosins; D008274:Magnesium; D003545:Cysteine; D005033:Ethylmaleimide