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April 15, 2004BiochemistryOpen Access

Poliovirus RNA-Dependent RNA Polymerase (3Dpol):  Pre-Steady-State Kinetic Analysis of Ribonucleotide Incorporation in the Presence of Mg2+

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Population

Poliovirus RNA-dependent RNA polymerase (3Dpol)

Comparison

Mn2+ as divalent cation cofactor vs Mg2+ as divalent cation cofactor

Design

Preclinical

Authors

JAJamie J. ArnoldUniversity of North Carolina at Chapel HillCCCraig E. CameronUniversity of North Carolina at Chapel Hill

Discussion

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Implication

Mn2+ may enable fidelity studies in viral polymerases; leaves open relevance to human antiviral design.

Structured PICO

P
Population
Poliovirus RNA-dependent RNA polymerase (3Dpol)
I
Intervention
Mn2+ as divalent cation cofactor
C
Comparator
Mg2+ as divalent cation cofactor
O
Outcome
Kinetic mechanism and rate of single nucleotide incorporation (phosphoryl transfer)surrogate

The study elucidates the biochemical mechanism by which Mn2+ reduces the fidelity of poliovirus RNA polymerase compared to Mg2+, highlighting the role of the phosphoryl-transfer step in nucleotide selection.

Cite This Study

Arnold et al. (2004) studied this question.

synapsesocial.com/papers/6a6fe215f44fa9f079dd60c9https://doi.org/10.1021/bi035212y
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