Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.7.7 (DNA polymerase)
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A previously described large Vermont kindred possessing a high incidence of venous thromboembolism with associated Type I protein C deficiency (1) has been genetically analyzed. All nine exons of the protein C gene, including both coding and non-coding regions, have been amplified from blood cell genomic DNA using the Tag DNA polymerase chain reaction (PCR) and primers corresponding to flanking intronic regions, and the products directly sequenced. An initial mutation (C-->T) resulting in Thr298-->Met was observed in one arm of the family exhibiting a history of thrombosis and protein C deficiency and was designated protein CVERMONT IIa. However, examination of the kindred member parent (male) of this arm and members of other arms of the kindred demonstrated that the mutation entered the arm via the genetically unrelated spouse. Further analysis of the father and members of other arms of the kindred revealed a different mutation (C insertion: CAT-->CCAT), resulting in a frameshift beginning at amino acid #107 (His-->Pro) and truncation of the protein at codon #119 of the mature protein. This mutation, called protein CVERMONT IIb, is associated with protein C deficiency and thrombosis throughout the kindred.
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PMID:Genetic analysis of a large kindred exhibiting type I protein C deficiency and associated thrombosis. 791 73

A low-abundance DNA-binding protein for the DNA polymerase beta (beta-pol) promoter initiator element was purified from bovine testis. The transcriptional initiator element (Inr) of the mammalian beta-pol promoters characterized is highly conserved, and the bovine beta-pol promoter Inr has the sequence -11CAGAGGCGGCCATTGTT+6. The purified initiator element-binding protein (Inr-BP) binds with high affinity to an oligonucleotide corresponding to the beta-pol promoter Inr (Kd = 5 pM), and increasing ionic strength decreases stability of the protein-DNA complex. Mutational analysis of the Inr shows that the purified Inr-BP binds with sequence specificity to the sequence CCAT at -2 to +2 of the Inr, but that seven residues on the 5' side and three residues on the 3' side of the CCAT sequence are required also. Using an in vitro transcription assay with HeLa cell nuclear extract, we find that the endogenous Inr-BP is required for transcriptional activity of the beta-pol promoter; addition of purified Inr-BP restores activity to the nuclear extract depleted in Inr-BP by affinity chromatography. These results, based upon the sequence specificity for DNA binding, indicate that Inr-BP is a YY1-like protein and suggest that it is a required transcription factor in beta-pol gene expression.
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PMID:Purification and characterization of a DNA polymerase beta promoter initiator element-binding transcription factor from bovine testis. 863 58