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Unlike the Escherichia coli counterpart, archaeal RNase HII cannot process ribose monophosphate abasic sites and oxidized ribonucleotides embedded in DNA ArchiMer
Malfatti, Matilde Clarissa; Henneke, Ghislaine; Balachander, Sathya; Koh, Kyung Duk; Newnam, Gary; Uehara, Ryo; Crouch, Robert J.; Storici, Francesca; Tell, Gianluca.
The presence of ribonucleoside monophosphates (rNMPs) in nuclear DNA decreases genome stability. To ensure survival despite rNMP insertions, cells have evolved a complex network of DNA repair mechanisms, in which the ribonucleotide excision repair pathway, initiated by type 2 ribonuclease H (RNase HII/2), plays a major role. We recently demonstrated that eukaryotic RNase H2 cannot repair damaged, that is, ribose monophosphate abasic (both apurinic or apyrimidinic) site (rAP) or oxidized rNMP embedded in DNA. Currently, it remains unclear why RNase H2 is unable to repair these modified nucleic acids having either only a sugar moiety or an oxidized base. Here, we compared the endoribonuclease specificity of the RNase HII enzymes from the archaeon Pyrococcus...
Tipo: Text Palavras-chave: Ribonuclease; Bacteria; Escherichia coli (E coli); Archaea; Oxidative stress; Abasic-ribose; Oxidized-ribonucleotides; Pyrococcus abyssi; Type 2 RNase H.
Ano: 2019 URL: https://archimer.ifremer.fr/doc/00506/61796/65801.pdf
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