N-Lobe Dynamics of Myosin Light Chain Dictates Its Mode of Interaction with Myosin V IQ1
Copyright policy )N-Lobe Dynamics of Myosin Light Chain Dictates Its Mode of Interaction with Myosin V IQ1
Myosin V motors regulate secretion and cell division in eukaryotes. How MyoV activity is differentially regulated by essential and calmodulin light chain binding remains unclear. We have used NMR spectroscopy to compare the dynamic behavior of Mlc1p, a budding yeast essential light chain, with that of the Xenopus laevis calmodulin. Both proteins have a similar structure and bind similar target proteins but differ in the mechanism by which they interact with the myosin V IQ1. This interaction is essential for MyoV activity. Here, we show that the rigid conformation of the loop connecting the two EF-hand motifs of the Mlc1p N-lobe explains its differential ability to interact with myosin V IQ1. Moreover, we show that the maintenance of the N-lobe structure is required for the essential function of Mlc1p in vivo. These data show that the core characteristics of myosin light chain N-lobes differentiate Mlc1p and calmodulin binding capability.
- University of Rome Tor Vergata Italy
- University of Parma Italy
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Models, Molecular, calmodulin, Magnetic Resonance Spectroscopy, Calmodulin binding, Amino Acid Motifs, Xenopus laevi, Molecular Conformation, budding, yeast, Dynamic behavior, Target protein, myosin V IQ1, Nuclear magnetic resonance, protein analysi, Models, binding affinity, Myosin v, Cell proliferation, Allele, Protein Stability, molecular dynamic, article, Essential light chain, unclassified drug, Phenotype, priority journal, protein protein interaction, Amino Acid Motif, Protein Binding, 570, Myosin Light Chains, Saccharomyces cerevisiae Proteins, Cell division, Cell Survival, myosin VI, Movement, Molecular Sequence Data, Myosin Type V, Saccharomyces cerevisiae, 530, in vivo study, Calmodulin, In-vivo, protein conformation, Cell proliferation; Flow interactions; Nuclear magnetic resonance; Proteins; Budding yeasts; Calmodulin bindings; Cell divisions; Dynamic behaviors; Essential light chains; In-vivo; Light chains; Lobe dynamics; Myosin light chains; Myosin v; Nmr spectroscopies; Target proteins; Xenopus laevis; Nuclear magnetic resonance spectroscopy; calmodulin; myosin light chain; myosin V IQ1; myosin VI; unclassified drug; amino acid sequence; article; binding affinity; budding; controlled study; in vivo study; light chain; molecular dynamics; nonhuman; nuclear magnetic resonance spectroscopy; priority journal; protein analysis; protein conformation; protein motif; protein protein interaction; protein structure; Xenopus laevis; yeast; Alleles; Amino Acid Motifs; Amino Acid Sequence; Animals; Calmodulin; Cell Survival; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Conformation; Molecular Sequence Data; Movement; Myosin Light Chains; Myosin Type V; Phenotype; Point Mutation; Protein Binding; Protein Stability; Protein Structure, Tertiary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Temperature; Xenopus Proteins; Eukaryota; Saccharomycetales; Xenopus laevis, Animals, Point Mutation, Budding yeast, controlled study, Amino Acid Sequence, protein structure, protein motif, Nuclear magnetic resonance spectroscopy, Alleles, Light chain, nonhuman, Animal, Protein, Molecular, Myosin light chain, Lobe dynamic, amino acid sequence, Protein Structure, Tertiary, Flow interaction, Nmr spectroscopie
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