FN Archimer Export Format
PT J
TI RNA processing machineries in Archaea: the 5′-3′ exoribonuclease aRNase J of the β-CASP family is engaged specifically with the helicase ASH-Ski2 and the 3′-5′ exoribonucleolytic RNA exosome machinery
BT 
AF Phung, Duy Khanh
   Etienne, Clarisse
   Batista, Manon
   Langendijk-Genevaux, Petra
   Moalic, Yann
   Laurent, Sebastien
   Liuu, Sophie
   Morales, Violette
   Jebbar, Mohamed
   Fichant, Gwennaele
   Bouvier, Marie
   Flament, Didier
   Clouet-d’Orval, Béatrice
AS 1:1;2:1;3:1;4:1;5:2;6:4;7:3;8:1;9:2;10:1;11:1;12:2;13:1;
FF 1:;2:;3:;4:;5:;6:PDG-REM-EEP-LMEE;7:;8:;9:;10:;11:;12:PDG-REM-EEP-LMEE;13:;
C1 Laboratoire de Microbiologie et de Génétique Moléculaires, UMR5100, Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, Université Paul Sabatier, F-31062 Toulouse, France
   Ifremer, Univ Brest, CNRS, Laboratoire de Microbiologie des Environnements Extrêmes, F-29280 Plouzané, France
   Micalis Institute, PAPPSO, INRA, AgroParisTech, Université Paris-Saclay, 78350, Jouy-en-Josas, France
   Ifremer, Univ Brest, CNRS, Laboratoire de Microbiologie des Environnements Extrêmes, F-29280 Plouzané, France
C2 CNRS, FRANCE
   IFREMER, FRANCE
   INRA, FRANCE
   UBO, FRANCE
SI BREST
SE PDG-REM-EEP-LMEE
UM BEEP-LM2E
IN WOS Ifremer UMR
   WOS Cotutelle UMR
   DOAJ
   copubli-france
   copubli-p187
   copubli-univ-france
IF 16.971
TC 14
UR https://archimer.ifremer.fr/doc/00610/72250/71056.pdf
   https://archimer.ifremer.fr/doc/00610/72250/71057.pdf
LA English
DT Article
AB A network of RNA helicases, endoribonucleases and exoribonucleases regulates the quantity and quality of cellular RNAs. To date, mechanistic studies focussed on bacterial and eukaryal systems due to the challenge of identifying the main drivers of RNA decay and processing in Archaea. Here, our data support that aRNase J, a 5′-3′ exoribonuclease of the β-CASP family conserved in Euryarchaeota, engages specifically with a Ski2-like helicase and the RNA exosome to potentially exert control over RNA surveillance, at the vicinity of the ribosome. Proteomic landscapes and direct protein–protein interaction analyses, strengthened by comprehensive phylogenomic studies demonstrated that aRNase J interplay with ASH-Ski2 and a cap exosome subunit. Finally, Thermococcus barophilus whole-cell extract fractionation experiments provide evidences that an aRNase J/ASH-Ski2 complex might exist in vivo and hint at an association of aRNase J with the ribosome that is emphasised in absence of ASH-Ski2. Whilst aRNase J homologues are found among bacteria, the RNA exosome and the Ski2-like RNA helicase have eukaryotic homologues, underlining the mosaic aspect of archaeal RNA machines. Altogether, these results suggest a fundamental role of β-CASP RNase/helicase complex in archaeal RNA metabolism. 
PY 2020
PD APR
SO Nucleic Acids Research
SN 0305-1048
PU Oxford University Press (OUP)
VL 48
IS 7
UT 000525957700035
BP 3832
EP 3847
DI 10.1093/nar/gkaa052
ID 72250
ER

EF