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Pausing kinetics dominates strand-displacement polymerization by reverse transcriptase
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DOI：10.1093/nar/gkx720.png)
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Abstract
En 中文
Reverse transcriptase (RT) catalyzes the conversion of the viral RNA into an integration-competent double-stranded DNA, with a variety of enzymatic activities that include the ability to displace a non-template strand concomitantly with polymerization. Here, using high-resolution optical tweezers to follow the activity of the murine leukemia Virus RT, we show that strand-displacement polymerization is frequently interrupted. Abundant pauses are modulated by the strength of the DNA duplex similar to 8 bp ahead, indicating the existence of uncharacterized RT/DNA interactions, and correspond to backtracking of the enzyme, whose recovery is also modulated by the duplex strength. Dissociation and reinitiation events, which induce long periods of inactivity and are likely the rate-limiting step in the synthesis of the genome in vivo, are modulated by the template structure and the viral nucleocapsid protein. Our results emphasize the potential regulatory role of conserved structural motifs, and may provide useful information for the development of potent and specific inhibitors.
Keywords:
MURINE LEUKEMIA-VIRUS
HIV-1 NUCLEOCAPSID PROTEIN
ACID CHAPERONE ACTIVITY
STEADY-STATE KINETICS
DNA-SYNTHESIS
CRYSTAL-STRUCTURE
OPTICAL TWEEZERS
SINGLE-MOLECULE
IN-VITRO
UNPAIRED NUCLEOTIDES
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