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The cDNAs coding for the α‐ and β‐subunits of Xenopus laevis casein kinase II
Author(s) -
Jedlicki Ana,
Hinrichs Maria Victoria,
Allende Catherine C.,
Allende Jorge E.
Publication year - 1992
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(92)80556-v
Subject(s) - xenopus , complementary dna , casein kinase 2 , biology , cdna library , microbiology and biotechnology , coding region , nucleic acid sequence , peptide sequence , amino acid , casein kinase 1 , protein subunit , biochemistry , gene , protein kinase a , kinase , cyclin dependent kinase 2
Using a λgt10 cDNA library obtained from Xenopus laevis oocytes and probes derived from the known sequences of the human and Drosophila genes, a cDNA coding for the α‐subunit of the X. laevis casein kinase II was isolated. The coding sequence of this clone determines a polypeptide of 350 amino acids. The X. laevis sequence is 98% identical to the human and rat proteins in the first 323 amino acids. Using the polymerase chain reaction to generate a 370‐nucleotide‐long probe, it was possible to clone and sequence a cDNA of 900 nucleotides that coded for the X. laevis β‐subunit of casein kinase II. The derived protein sequence is 215 amino acids long and again shows an extraordinary degree of conservation with other species.