Characterization and bacterial expression of the Dictyostelium myosin light chain kinase cDNA. Identification of an autoinhibitory domain.
作者： J.L. Tan , J.A. Spudich
DOI: 10.1016/S0021-9258(18)98513-3
关键词:
摘要: A full-length cDNA corresponding to the Dictyostelium myosin light chain kinase gene has been isolated and characterized. Sequence analysis of confirms conserved protein subdomains reveals that sequence is highly homologous those calcium/calmodulin-dependent kinases, including kinases from higher eukaryotes. Despite high homologies there no recognizable calmodulin-binding domain within sequence. However, possesses a putative auto-inhibitory near its carboxyl terminus. To further characterize this domain, enzyme as well truncated form lacking were expressed in bacterial cells purified. The bacteria exhibits essentially same biochemical characteristics Dictyostelium. however Vmax approximately ten times greater than native enzyme. In addition, unlike bacteria, does not undergo autophosphorylation. These results suggest enzyme, like eukaryotes, regulated by an autoinhibitory but specific molecular signals necessary for activation are entirely distinct.
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