Six putative IQ motifs of the recombinant chicken intestinal brush border myosin I are involved in calmodulin binding.

Chicken brush border myosin I has up to six IQ sequence motifs at which it may bind calmodulin. To determine the relative contributions of these motifs to calmodulin binding, fusion deletion fragments were expressed in Escherichia coli and their ability to bind calmodulin was assessed by the gel overlay technique. The first three N-terminal IQ sites showed strong binding with calmodulin. Surprisingly, the last three incomplete IQ motifs also contributed substantial calmodulin binding. The first and fourth IQ sites bound calmodulin but tended to reduce binding in combination with other sites. The data indicate that interactions among all six IQ motifs contribute to the ability of myosin I to bind calmodulin.

[1]  A. Houdusse,et al.  A model of Ca(2+)-free calmodulin binding to unconventional myosins reveals how calmodulin acts as a regulatory switch. , 1996, Structure.

[2]  L. Komuves,et al.  Zipper Protein, a B-G Protein with the Ability to Regulate Actin/Myosin 1 Interactions in the Intestinal Brush Border (*) , 1996, The Journal of Biological Chemistry.

[3]  J. Wolenski Regulation of calmodulin-binding myosins. , 1995, Trends in cell biology.

[4]  H. Zot Phospholipid membrane-associated brush border myosin-I activity. , 1995, Cell motility and the cytoskeleton.

[5]  P. Matsudaira,et al.  Recombinant expression of the brush border myosin I heavy chain. , 1995, Cell motility and the cytoskeleton.

[6]  M. Bähler,et al.  Rat myr 4 defines a novel subclass of myosin I: identification, distribution, localization, and mapping of calmodulin-binding sites with differential calcium sensitivity , 1994, The Journal of cell biology.

[7]  D. Bikle,et al.  Regulation of calmodulin binding to the ATP extractable 110 kDa protein (myosin I) from chicken duodenal brush border by 1,25-(OH)2D3. , 1994, Biochimica et biophysica acta.

[8]  T. Davis,et al.  The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth in Saccharomyces cerevisiae , 1994, The Journal of cell biology.

[9]  H. Swanljung-Collins,et al.  Brush border myosin I has a calmodulin/phosphatidylserine switch and tail actin-binding. , 1994, Advances in experimental medicine and biology.

[10]  P. Forscher,et al.  Calcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry , 1993, The Journal of cell biology.

[11]  M. Bähler,et al.  Identification, characterization and cloning of myr 1, a mammalian myosin-I , 1993, The Journal of cell biology.

[12]  H. Swanljung-Collins,et al.  Phosphorylation of brush border myosin I by protein kinase C is regulated by Ca(2+)-stimulated binding of myosin I to phosphatidylserine concerted with calmodulin dissociation. , 1992, The Journal of biological chemistry.

[13]  H. Swanljung-Collins,et al.  Ca2+ stimulates the Mg2(+)-ATPase activity of brush border myosin I with three or four calmodulin light chains but inhibits with less than two bound. , 1991, The Journal of biological chemistry.

[14]  J. Wolenski,et al.  Binding of brush border myosin I to phospholipid vesicles , 1990, The Journal of cell biology.

[15]  J. Sellers,et al.  Calmodulin dissociation regulates brush border myosin I (110-kD- calmodulin) mechanochemical activity in vitro , 1990, The Journal of cell biology.

[16]  M. Arpin,et al.  Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus shows that this mechanoenzyme is a member of the myosin I family , 1989, The Journal of cell biology.

[17]  M. Mooseker,et al.  The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin I) is a mechanoenzyme , 1989, The Journal of cell biology.

[18]  D. Bikle,et al.  The villus gradient of brush border membrane calmodulin and the calcium-independent calmodulin-binding protein parallels that of calcium-accumulating ability. , 1986, Endocrinology.

[19]  D. Bikle,et al.  1,25-Dihydroxyvitamin D increases calmodulin binding to specific proteins in the chick duodenal brush border membrane. , 1985, The Journal of clinical investigation.

[20]  J. Chafouleas,et al.  Calmodulin may mediate 1,25‐dihydroxyvitamin D‐stimulated intestinal calcium transport , 1984, FEBS letters.

[21]  J. Chafouleas,et al.  Calmodulin-Binding Proteins in a Cloned Rat Insulinoma Cell Line , 1983, Diabetes.

[22]  D. Bikle,et al.  Calcium flux across chick duodenal brush border membrane vesicles: regulation by 1,25-dihydroxyvitamin D. , 1983, Endocrinology.

[23]  L. Orci,et al.  Immunocytochemical localization of the vitamin D-dependent calcium binding protein in chick duodenum , 1982, The Journal of cell biology.

[24]  K. Weber,et al.  Calmodulin-binding proteins of the microfilaments present in isolated brush borders and microvilli of intestinal epithelial cells. , 1980, The Journal of biological chemistry.

[25]  M. M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[26]  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.

[27]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[28]  O. H. Lowry,et al.  Protein measurement with the Folin phenol reagent. , 1951, The Journal of biological chemistry.