Isolation and sequencing of cDNA clones encoding alpha and beta subunits of Drosophila melanogaster casein kinase II.

AUTOR(ES)

Saxena, A

RESUMO

Cloned cDNAs encoding both subunits of Drosophila melanogaster casein kinase II have been isolated by immunological screening of lambda gt11 expression libraries, and the complete amino acid sequence of both polypeptides has been deduced by DNA sequencing. The alpha cDNA contained an open reading frame of 336 amino acid residues, yielding a predicted molecular weight for the alpha polypeptide of 39,833. The alpha sequence contained the expected semi-invariant residues present in the catalytic domain of previously sequenced protein kinases, confirming that it is the catalytic subunit of the enzyme. Pairwise homology comparisons between the alpha sequence and the sequences of a variety of vertebrate protein kinase suggested that casein kinase II is a distantly related member of the protein kinase family. The beta subunit was derived from an open reading frame of 215 amino acid residues and was predicted to have a molecular weight of 24,700. The beta subunit exhibited no extensive homology to other proteins whose sequences are currently known.

Documentos Relacionados

• The nucleotide sequence of the mouse cDNA encoding the beta subunit of casein kinase II.
• Isolation of genomic and cDNA clones encoding bovine poly(A) binding protein II.
• Isolation, sequencing, and disruption of the CKA1 gene encoding the alpha subunit of yeast casein kinase II.
• Isolation of cDNA clones encoding HLA-DR alpha chains.
• Isolation of cDNA and genomic DNA clones encoding type II collagen.