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pubmed-article:2437438pubmed:abstractTextAn attempt to study the functional role of one of the most conservative domains found in all RNA-dependent RNA and DNA polymerases of plant and animal viruses (the so called "DD-domain") was made. A structure similar to the "DD-domain" was found in a minor T7 phage tail protein--gpII. Antibodies against this phage protein have been raised and used to probe "DD-domain" in molecules of avian myeloblastose virus reverse transcriptase and E. coli RNA-dependent RNA polymerase. The antibodies are shown to inhibit the activity of these enzymes under certain conditions. At the same time inhibition of the reverse transcriptase reaction causes the decrease in length of the most high molecular cDNA-products as well. The experimental data obtained are discussed in view of the suggested hypothesis on the probable functional role of the "DD-domain" of RNA-dependent polymerases.lld:pubmed
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pubmed-article:2437438pubmed:authorpubmed-author:ZavrievS KSKlld:pubmed
pubmed-article:2437438pubmed:authorpubmed-author:BorisovaO VOVlld:pubmed
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pubmed-article:2437438pubmed:pagination229-41lld:pubmed
pubmed-article:2437438pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:2437438pubmed:articleTitle[Possible functional role of the DD-domain of RNA-dependent polymerases].lld:pubmed
pubmed-article:2437438pubmed:publicationTypeJournal Articlelld:pubmed
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