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  • 1
    ISSN: 1432-1424
    Keywords: calmodulin ; mutation ; ion currents ; Paramecium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Two behavioral mutants ofParamecium tetraurelia, pantophobiacs A1 and A2, have single amino acid defects in the structure of calmodulin. The mutants exhibit several major ion current defects under voltage clamp: (i) the Ca2+-dependent K+ current activated upon depolarization ofParamecium is greatly reduced or missing in both mutants, (ii) both mutants lack a Ca2+-dependent K+ current activated upon hyperpolarization, and (iii) the Ca2+-dependent Na+ current is significantly smaller in pantophobiac A1 compared with the wild type, whereas this current is slightly increased in pantophobiac A2. Other, minor defects include a reduction in peak amplitude of the depolarization-activated Ca2+ current in pantophobiac A2, increased rates of voltage-dependent inactivation of this Ca2+ current in both pantophobiac A1 and pantophobiac A2, and an increase in the time required for the hyperpolarization-activated Ca2+ current to recover from inactivation in the pantophobiacs. The diversity of the pantophobiac mutations' effects on ion current function may indicate specific associations of calmodulin with a variety of Ca2+-related ion channel species inParamecium.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1424
    Keywords: calmodulin ; Ca2+-dependent K+ channels ; ion channel regulation ; mutations ; Paramecium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Paramecium tetraurelia possesses two Ca2+-dependent K+ currents, activated upon depolarizationI K(Ca,d), or upon hyperpolarizationI K(Ca,h). The two currents are mediated by pharmacologically distinct ion channel populations. Three mutations ofP. tetraurelia affect these current.s Pantophobiac A mutations (pntA) cause calmodulin sequence defects, resulting in the loss of both Ca2+-dependent K+ currents. A second mutation, TEA-insensitive A (teaA), greatly enhancesI K(Ca,d) but has no affect onI K(Ca,h). A third mutation,restless (rst), also increasesI K(Ca,d) slightly, but its principle effect is in causing an early activation ofI K(Ca,h). Interactions between the products of these three genes were investigated by constructing three double mutants. BothteaA andrst restoreI K(Ca,d) andI K(Ca,h) in pantophobiac A1, but the phenotypes ofteaA andrst are not corrected by a second mutation. These observations may indicate a role for the gene products ofteaA andrst in regulating the activity ofI K(Ca,d) andI K(Ca,h), respectively.
    Type of Medium: Electronic Resource
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