Meh Sameen Nawaz

Loading metrics Open Access Peer-reviewed Research Article Natalia Berges, Meh Sameen Nawaz, Tuva Børresdatter Dahl, Lars Hagen, Magnar Bjørås, Jon K. Laerdahl, Ingrun Alseth Natalia Berges, Meh Sameen Nawaz, Tuva Børresdatter Dahl, Lars Hagen, Magnar Bjørås, Jon K. Laerdahl, Ingrun Alseth Published: November 8, 2019 https://doi.org/10.1371/journal.pone.0225081 Figures Abstract Endonuclease V (ENDOV) is a ribonuclease with affinity for inosine which is the deamination product of adenosine.

Endonuclease V (EndoV) is an enzyme with specificity for inosines in nucleic acids. Whereas the bacterial homologs are active on both DNA and RNA, the mammalian variants only cleave RNA, at least when assayed with recombinant proteins. Here we show that ectopically expressed, as well as endogenously expressed human (h)EndoV, share the same enzymatic properties as the recombinant protein and cleaves RNA with inosine but not DNA.

Endonuclease V (EndoV) is an enzyme with specificity for inosines in nucleic acids. Whereas the bacterial homologs are active on both DNA and RNA, the mammalian variants only cleave RNA, at least when assayed with recombinant proteins. Here we show that ectopically expressed, as well as endogenously expressed human (h)EndoV, share the same enzymatic properties as the recombinant protein and cleaves RNA with inosine but not DNA.