Recombinant DNA techniques in a scallop myosin model reveal that a high-affinity metal binding site in the N-terminal domain and its interaction with C-terminal domains are essential for regulatory light chain function.
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The ability to exchange reversibly the regulatory light chains (RLCs) from scallop myosin has provided us with a test system to probe the mechanisms of regulation mediated by the RLCs from vertebrate skeletal, vertebrate smooth and molluscan myosins. The cloning and expression of these RLCs, together with domain-swapping and site-directed mutagenesis approaches, has allowed us to explore further the mechanisms involved and identify the functional importance of specific regions of the RLC molecule; for example, the presence of a high affinity metal binding site in the N-terminal domain and its interaction with the intact C-terminal domains are required for regulation.
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Findings limited to scallop myosin; leaves open relevance to mammalian cardiac regulation.
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Kendrick‐Jones et al. (1991) studied this question.
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