Disease relevance of DNApol-alpha73

• We compared the fidelity of copying mC versus C and the efficiency of extending mismatched base pairs at the mC position using three DNA polymerases, AMV reverse transcriptase, Drosophila DNA polymerase alpha, and mutant Escherichia coli Klenow fragment containing no proofreading exonuclease activity [1].

High impact information on DNApol-alpha73

• An analysis was carried out on the promoter region of the Drosophila DNA polymerase alpha 73-kDa subunit gene and the factor(s) activating the promoter [2].
• The DRE/DREF system plays an important role in transcription of DNA replication genes such as those encoding the 180 and 73 kDa subunits of DNA polymerase alpha as well as that for encoding PCNA [3].
• A transcription unit was identified in the 43E polytene band region of the second chromosome of Drosophila melanogaster (Dm) whose putative translation product has 85% amino acid (aa) identity with the B subunit of the calcineurin protein (CnB) from humans [4].
• Phosphorylation and dephosphorylation of the B subunit of DNA polymerase alpha-primase complex in the early embryogenesis of Drosophila [5].
• Lambda phosphatase treatment showed that the reduced migration was caused by phosphorylation of the B subunit [5].

Biological context of DNApol-alpha73

• The amino acid sequence (458 amino acids; Mr, 51,308) of B subunit of the M-12 enzyme was 74%, 53%, 52% and 54% identical with those of the ATPases from E. hirae, T. thermophilus, N. crassa and D. melanogaster, respectively [6].

Other interactions of DNApol-alpha73

• The kinase will phosphorylate histone H1, but prefers peptides contained in the DNA polymerase alpha-kinase complex [7].

Analytical, diagnostic and therapeutic context of DNApol-alpha73

• We report that Drosophila embryo DNA polymerase alpha complex, isolated by immunological techniques, contains a protein kinase activity [7].

References