High Affinity Divalent Cation Binding to Actin
نویسندگان
چکیده
منابع مشابه
Nonselective, Low Affinity Divalent Cation Site
The ability of membrane voltage to activate high conductance, calcium-activated (BK-type) K channels is enhanced by cytosolic calcium (Ca 2 ). Activation is sensitive to a range of [Ca 2 ] that spans over four orders of magnitude. Here, we examine the activation of BK channels resulting from expression of cloned mouse Slo1 subunits at [Ca 2 ] and [Mg 2 ] up to 100 mM. The half-activation voltag...
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Sites with high calcium affinity in Paramecium aurelia were identified by high calcium (5 mM) fixation and electron microscope methods. Electron-opaque deposits were observed on the cytoplasmic side of surface membranes, particularly at the basal regions of cilia and trichocyst-pellicle fusion sites. Deposits were also observed on some smooth cytomembranes, within the axoneme of cilia, and on b...
متن کاملThe Binding of Divalent Cations to Actin.
Great effort has been spent in recent years on the investigation of certain aspects of actin polymerization, such as the dephosphorylation of adenosine triphosphate during G to F transformation (l-6), the mode of interaction of ATP with actin (i-15), and the role of sulfhydryl, histidine, tyrosine, and other groups in the polymerization process (8-10, 12-14, 16-18). It has been found that actin...
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Single channel currents from recombinant N-methyl-D-aspartate (NMDA) receptors having an N-to-Q mutation in M2 reveal a divalent cation binding site that is near the entrance of the pore (approximately 0.2 through the electric field). Ca2+ rapidly binds to this site and readily permeates the channel, while Mg2+ binds more slowly and does not permeate as readily. In wild-type receptors, Mg2+ als...
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Sequence-specific binding of divalent cations to nucleosomal DNA can potentially influence nucleosome position and mobility, as well as modulate interactions with nuclear factors. We define the bonding and specificity of divalent cation interaction with nucleosomal DNA by characterizing Mn2+ binding in the x-ray structure of the nucleosome core particle at 1.9-A resolution. Manganese ions are f...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)60525-3