Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.7.7 (DNA polymerase)
 17,007 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Human HBV polymerase has been expressed in reticulocyte lysate system. The expressed protein shows the DNA-dependent DNA polymerase activity. In vitro transcription and translation produces a major protein product with an apparent molecular weight of approximately 100 kD. The HBV DNA polymerase has been characterized biochemically in the condition that the contaminating cellular DNA polymerases were fairly suppressed by aphidicolin and NEM. The polymerization reaction is optimal at pH 7.5 and 37 degrees C and the polymerase requires either MnCl2 or MgCl2, with a preference for MnCl2. The protein represented an optimal activity in the presence of either 75 mM NaCl or 100 mM KCl, with a higher activity at 75 mM NaCl than 100 mM KCl. Study of the polymerizing activity of the deleted versions of the polymerase protein suggests that the terminal protein is essential for full polymerase function and the spacer region may decrease the stability of the P protein.
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PMID:Active human hepatitis B viral polymerase expressed in rabbit reticulocyte lysate system. 1054 Oct 16

mus 308 designates one of over 30 mutagen sensitivity loci found in Drosophila. It is predicted to code for a 229-kDa polypeptide. Published sequence analyses of others indicate that this polypeptide would have helicase motifs near its N-terminus, and similarities to bacterial DNA polymerase I-like enzymes near its C-terminus. In our studies, two different and highly specific antibodies were prepared and used for identification as well as characterization of the mus 308 gene product. Western blot analyses reveal a single reactive polypeptide in both ovaries and embryos as well as in two Drosophila embryo tissue culture cell lines; it is nearly absent in homozygous mus 308 mutants. This polypeptide is about 229 kDa in size, and indirect immunofluorescence shows that the mus 308 gene product localizes throughout nuclei in wild-type cells but appears to be absent in a mus 308 mutant. Immunoblot analyses throughout development suggest greatest abundance at the end of embryogenesis, immediately before hatching of first instar larvae. They also showed a smaller ( approximately 100 kDa) antigenically and genetically related polypeptide found only in adult males. Immunoprecipitation, a highly effective method of specific purification, suggests that the mus 308 protein has DNA polymerase activity that is NEM-sensitive but largely aphidicolin-resistant. In addition, the immunoprecipitated material has DNA-dependent ATPase but lacks detectable helicase.
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PMID:The Drosophila mus 308 gene product, implicated in tolerance of DNA interstrand crosslinks, is a nuclear protein found in both ovaries and embryos. 1596 55


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