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Isolation and sequence analysis of a cDNA clone encoding the entire catalytic subunit of phosphorylase kinase
Author(s) -
da Cruz e Silva Edgar F.,
Cohen Patricia T.W.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80871-2
Subject(s) - phosphorylase kinase , complementary dna , biology , cdna library , microbiology and biotechnology , peptide sequence , nucleic acid sequence , protein subunit , biochemistry , sequence analysis , clone (java method) , oligonucleotide , coding region , genetics , gene
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 λgt10. 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.