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Incorporation of deoxyribonucleotides and ribonucleotides by a dNTP-binding cleft mutated reverse transcriptase in hepatitis B virus core particles.

Authors
Kim, HY; Jung, J; Park, S; Shin, HJ; Kim, K
Citation
Virology, 370(1):205-212, 2008
Journal Title
Virology
ISSN
0042-68221096-0341
Abstract
Our recent observation that hepatitis B virus (HBV) DNA polymerase (P) might initiate minus-strand DNA synthesis without primer [Kim et al., (2004) Virology 322, 22-30], raised a possibility that HBV P protein may have the potential to function as an RNA polymerase. Thus, we mutated Phe 436, a bulky amino acid with aromatic side chain, at the putative dNTP-binding cleft in reverse transcriptase (RT) domain of P protein to smaller amino acids (Gly or Val), and examined RNA polymerase activity. HBV core particles containing RT dNTP-binding cleft mutant P protein were able to incorporate (32)P-ribonucleotides, but not HBV core particles containing wild type (wt), priming-deficient mutant, or RT-deficient mutant P proteins. Since all the experiments were conducted with core particles isolated from transfected cells, our results indicate that the HBV RT mutant core particles containing RT dNTP-binding cleft mutant P protein could incorporate both deoxyribonucleotides and ribonucleotides in replicating systems.
MeSH terms
Cell Line, TumorDeoxyribonucleotides/geneticsDeoxyribonucleotides/metabolism*Gene Products, pol/geneticsGene Products, pol/metabolismHepatitis B virus/enzymology*Hepatitis B virus/geneticsHumansMutation*RNA-Directed DNA Polymerase/chemistryRNA-Directed DNA Polymerase/genetics*RNA-Directed DNA Polymerase/metabolismRibonucleotides/geneticsRibonucleotides/metabolism*Virion/metabolism*
DOI
10.1016/j.virol.2007.08.018
PMID
17900649
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Microbiology
AJOU Authors
박선신호준김경민
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