The cDNAs coding for the alpha- and beta-subunits of Xenopus laevis casein kinase II.
Using a lambda gt10 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 alpha-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 beta-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.
Jedlicki
A
A
Departamento de Bioquímica, Facultad de Medicina, Universidad de Chile, Santiago.
Hinrichs
M V
MV
Allende
C C
CC
Allende
J E
JE
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D047390:Casein Kinase II; D003001:Cloning, Molecular; D004247:DNA; D006801:Humans; D008969:Molecular Sequence Data; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D014982:Xenopus laevis
D004247:DNA; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases