FN Archimer Export Format
PT J
TI Unlike the Escherichia coli counterpart, archaeal RNase HII cannot process ribose monophosphate abasic sites and oxidized ribonucleotides embedded in DNA
BT 
AF Malfatti, Matilde Clarissa
   Henneke, Ghislaine
   Balachander, Sathya
   Koh, Kyung Duk
   Newnam, Gary
   Uehara, Ryo
   Crouch, Robert J.
   Storici, Francesca
   Tell, Gianluca
AS 1:1;2:2;3:3;4:4;5:3;6:5;7:6;8:3;9:1;
FF 1:;2:PDG-REM-EEP-LMEE;3:;4:;5:;6:;7:;8:;9:;
C1 University of Udine, Italy
   Ifremer, Univ Brest, CNRS, Laboratoire de Microbiologie des Environnements Extrêmes, France
   School of Biological Sciences, Georgia Institute of Technology, United States
   Lung Biology Center, Department of Medicine, University of California, San Francisco, San Francisco, CA, United States
   Ritsumeikan Global Innovation Research Organization, Ritsumeikan University, 1-1-1 Noji-higashi, Kusatsu, Shiga 525-8577, Japan
   Eunice Kennedy Shriver National Institute of Child Health and Human Developement
C2 UNIV UDINE, ITALY
   IFREMER, FRANCE
   GEORGIA INST TECHNOL, USA
   UNIV CALIF SAN FRANCISCO, USA
   UNIV RITSUMEIKAN, JAPAN
   NICHD, USA
SI BREST
SE PDG-REM-EEP-LMEE
UM BEEP-LM2E
IN WOS Ifremer UMR
   copubli-europe
   copubli-int-hors-europe
IF 4.238
TC 12
UR https://archimer.ifremer.fr/doc/00506/61796/65801.pdf
LA English
DT Article
DE ;ribonuclease;bacteria;Escherichia coli (E coli);archaea;oxidative stress;abasic-ribose;oxidized-ribonucleotides;Pyrococcus abyssi;Type 2 RNase H
AB 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 abyssi and the bacterium Escherichia coli, examining their ability to process damaged rNMPs embedded in DNA in vitro. We found that E. coli RNase HII cleaves both rAP and oxidized rNMP sites. In contrast, like the eukaryotic RNase H2, P. abyssi RNase HII did not display any rAP or oxidized rNMP incision activities, even though it recognized them. Notably, the archaeal enzyme was also inactive on a mismatched rNMP, whereas the E. coli enzyme displayed strong preference for the mispaired rNMP over the paired rNMP in DNA. On the basis of our biochemical findings and also structural modeling analyses of RNase HII/2 proteins from organisms belonging to all three domains of life, we propose that RNases HII/2’s dual roles in RER and RNA/DNA hydrolysis result in limited acceptance of modified rNMPs embedded in DNA. 
PY 2019
PD AUG
SO Journal Of Biological Chemistry
SN 0021-9258
PU American Society for Biochemistry & Molecular Biology (ASBMB)
VL 294
IS 35
UT 000486416000017
BP 13061
EP 13072
DI 10.1074/jbc.RA119.009493
ID 61796
ER

EF