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Two exons encode the calmodulin-binding domain in the mouse phosphorylase kinase catalytic subunit gene
Affiliation:1. From the Department of Biochemistry and Nutrition, Virginia Polytechnic Institute, Blacksburg, Virginia, USA;2. Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA;3. Department of Biochemistry University of Tennessee, Memphis, Tennessee, USA
Abstract:The catalytic subunit, γ, of phosphorylase kinase contains two calmodulin-binding sequences that define a domain in γ that is homologous to the troponin-C-binding domain in troponin I. The homology is based on both sequence and functional similarities. To account for this homology, it has been proposed that the calmodulin-binding sequences in γ and the troponin-C-binding domain in troponin I have evolved from a common ancestor. We investigated this possibility by comparing the exon structure of the γ gene with that of the troponin-I gene over their homologous domains. In the quail troponin-I gene, it is known that the entire troponin-C-binding domain is encoded by a single exon. However, two exons are found to encode the calmodulin-binding domain in the γ gene from mouse. This result indicates that convergent evolution may be responsible for the sequence and functional similarities between the homologous domains in troponin I and γ.
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