A novel biosensor for mercuric ions based on motor proteins

We explored the potential for use of the contractile proteins, actin and myosin, as biosensors of solutions containing mercury ions. We demonstrate that the reaction of HgCl2 with myosin rapidly inhibits actin-activated myosin ATPase activity. Mercuric ions inhibit the in vitro analog of contraction, namely the ATP-initiated superprecipitation of the reconstituted actomyosin complex. Hg reduces both the rate and extent of this reaction. Direct observation of the propulsive movement of actin filaments (10 nm in diameter and 1 μm long) in a motility assay driven by a proteolytic fragment of myosin (heavy meromyosin or HMM) is also inhibited by mercuric ions. Thus, we have demonstrated the biochemical, biophysical and nanotechnological basis of what may prove to be a useful nano-device.

[1]  W. Kabsch,et al.  Atomic structure of the actin: DNase I complex , 1990, Nature.

[2]  J. Spudich,et al.  The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. , 1971, The Journal of biological chemistry.

[3]  S. Lowey,et al.  Interaction of myosin subfragments with F-actin. , 1978, Biochemistry.

[4]  R. Cooke,et al.  Actomyosin interaction in striated muscle. , 1997, Physiological reviews.

[5]  Herbert R. Wilson,et al.  Diffraction of X-rays by proteins, nucleic acids and viruses , 1966 .

[6]  C. Bonan,et al.  Effects of mercury on myosin ATPase in the ventricular myocardium of the rat. , 2003, Comparative biochemistry and physiology. Toxicology & pharmacology : CBP.

[7]  E. Eisenberg,et al.  Interaction of SH 1 -blocked HMM with actin and ATP. , 1972, Nature: New biology.

[8]  S. Ebashi,et al.  Calcium binding activity of vesicular relaxing factor. , 1961, Journal de chirurgie.

[9]  Diana J. Oakes,et al.  Environmental Applications with Submitochondrial Particles , 2005 .

[10]  D. V. Vassallo,et al.  Effects of mercury on the isolated heart muscle are prevented by DTT and cysteine. , 1999, Toxicology and applied pharmacology.

[11]  Roberto Todeschini,et al.  Submitochondrial particles as toxicity biosensors of chlorophenols , 1995 .

[12]  C. D. dos Remedios,et al.  Actin binding proteins: regulation of cytoskeletal microfilaments. , 2003, Physiological reviews.

[13]  P. V. von Hippel,et al.  On the molecular weight of myosin. , 1958, Biochimica et biophysica acta.

[14]  K. Nagano,et al.  The Sodium- and Potassium-Activated Adenosinetriphosphatase System , 1971 .

[15]  S Halbach Sulfhydryl-induced restoration of myocardial contractility after alteration by mercury. , 1989, Archives of toxicology. Supplement. = Archiv fur Toxikologie. Supplement.

[16]  J. Harkin,et al.  Mammalian mitochondria asin vitro monitors of water quality , 1987, Bulletin of environmental contamination and toxicology.