Isolation and sequence analysis of a cDNA clone encoding the entire catalytic subunit of phosphorylase kinase.
Synthetic oligonucleotides have been used to isolate a 1.85 kb clone containing the full length coding sequence for the catalytic subunit of rabbit skeletal muscle phosphorylase kinase from a cDNA library constructed in lambda gt10. Sequence analysis of the clone predicted an amino acid sequence in agreement with a published primary structure. Inspection of the codon usage revealed a strong preference for G or C nucleotides at the third codon position as found for several other skeletal muscle proteins. This cDNA clone should facilitate identification of functional domains, including the calmodulin-binding site, and investigation of the molecular basis of X-linked phosphorylase kinase deficiencies.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002384:Catalysis; D003001:Cloning, Molecular; D003062:Codon; D004247:DNA / Q000302:isolation & purification*; D009132:Muscles / Q000201:enzymology; D010764:Phosphorylase Kinase / Q000032:analysis / Q000235:genetics*; D011817:Rabbits
D003062:Codon; D004247:DNA; D010764:Phosphorylase Kinase