Anomalous Reverse Transcription through Chemical Modifications in Polyadenosine Stretches.

ABSTRACT: Thermostable reverse transcriptases are workhorse enzymes underlying nearly all modern techniques for RNA structure mapping and for the transcriptome-wide discovery of RNA chemical modifications. Despite their wide use, these enzymes' behaviors at chemical modified nucleotides remain poorly understood. Wellington-Oguri et al. recently reported an apparent loss of chemical modification within putatively unstructured polyadenosine stretches modified by dimethyl sulfate or 2' hydroxyl acylation, as probed by reverse transcription. Here, reanalysis of these and other publicly available data, capillary electrophoresis experiments on chemically modified RNAs, and nuclear magnetic resonance spectroscopy on (A)₁₂ and variants show that this effect is unlikely to arise from an unusual st

SUBMITTER: Kladwang W 

PROVIDER: S-EPMC8118224 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature