RNase H is an exo- and endoribonuclease with asymmetric directionality, depending on the binding mode to the structural variants of RNA:DNA hybrids

Hyunjee Lee, HyeokJin Cho, Jooyoung Kim, Sua Lee, Jungmin Yoo, Daeho Park, and Gwangrog Lee

Nucleic Acids Research (2021) doi:10.1093/nar/gkab1064

A team of investigators led by Dr. GwanRog Lee at the Gwangju Institute of Science and Technology (Korea) describe a comprehensive analysis of RNA:DNA hybrid processing by RNase H using single-molecule FRET (smFRET). The work provides a significant advance in the fundamental understanding of the multifunctional activity of RNase H on structural variants of RNA:DNA hybrids. Most importantly, the study indicates that 5’-to-3’ directional and processive exonuclease activity, rather than the previously reported nonspecific endonuclease activity, is the primary physiological degradation mode since 3’ ssDNA overhangs are always present during RNA elimination by RNase H.

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