The catalytic properties of the recombinant reverse transcriptase of bovine immunodeficiency virus
| Autor: | Orna Avidan, Ron Bochner, Amnon Hizi |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Gene Expression Regulation
Viral Immunodeficiency Virus Bovine DNA polymerase Molecular Sequence Data Ribonuclease H Lentiviruses Catalysis Gene Expression Regulation Enzymologic law.invention Retrovirus law Virology Reverse transcriptase Amino Acid Sequence RNase H Polymerase biology Human immunodeficiency virus Bovine immunodeficiency virus RNA-Directed DNA Polymerase Processivity biology.organism_classification Molecular biology Recombinant Proteins Protease DNA Viral biology.protein Recombinant DNA Plasmids |
| Zdroj: | Virology. 351(1):42-57 |
| ISSN: | 0042-6822 |
| DOI: | 10.1016/j.virol.2006.03.012 |
| Popis: | Bovine immunodeficiency virus (BIV) is a lentivirus with no proven pathogenesis in infected cattle. Yet, in experimentally infected rabbits, it causes an AIDS-like disease. Consequently, we expressed two recombinant isoforms of BIV reverse transcriptase (RT), which differ in their C-termini, and studied their catalytic properties. Both isoforms prefer Mg+2 over Mn+2 with most DNA polymerase and ribonuclease-H substrates. The processivity of DNA synthesis by the BIV RTs is higher than that of HIV-1 RT, whereas the fidelity of synthesis is even lower than that of the HIV-1 enzyme. The ribonuclease-H cleavage pattern suggests that the spatial distance between the polymerase and ribonuclease-H active sites of the two BIV RT isoforms equals 20 nt, unlike the 17 nt distance observed in almost all other RTs. The longer BIV RT version is somewhat less active than the shorter version, suggesting that the extra 74 residues (with homology to dUTPases) might obstruct efficient catalysis. |
| Databáze: | OpenAIRE |
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