TY - JOUR
T1 - Mapping domains of ARS2 critical for its RNA decay capacity
AU - Melko, Mireille
AU - Winczura, Kinga
AU - Rouvière, Jérôme Olivier
AU - Oborská-Oplová, Michaela
AU - Andersen, Pia K.
AU - Heick Jensen, Torben
PY - 2020/7
Y1 - 2020/7
N2 - ARS2 is a conserved protein centrally involved in both nuclear RNA productive and destructive processes. To map features of ARS2 promoting RNA decay, we utilized two different RNA reporters, one of which depends on direct ARS2 tethering for its degradation. In both cases, ARS2 triggers a degradation phenotype aided by its interaction with the poly(A) tail exosome targeting (PAXT) connection. Interestingly, C-terminal amino acids of ARS2, responsible for binding the RNA 5'cap binding complex (CBC), become dispensable when ARS2 is directly tethered to the reporter RNA. In contrast, the Zinc-finger (ZnF) domain of ARS2 is essential for the decay of both reporters and consistently co-immunoprecipitation analyses reveal a necessity of this domain for the interaction of ARS2 with the PAXT-associated RNA helicase MTR4. Taken together, our results map the domains of ARS2 underlying two essential properties of the protein: its RNP targeting ability and its capacity to recruit the RNA decay machinery.
AB - ARS2 is a conserved protein centrally involved in both nuclear RNA productive and destructive processes. To map features of ARS2 promoting RNA decay, we utilized two different RNA reporters, one of which depends on direct ARS2 tethering for its degradation. In both cases, ARS2 triggers a degradation phenotype aided by its interaction with the poly(A) tail exosome targeting (PAXT) connection. Interestingly, C-terminal amino acids of ARS2, responsible for binding the RNA 5'cap binding complex (CBC), become dispensable when ARS2 is directly tethered to the reporter RNA. In contrast, the Zinc-finger (ZnF) domain of ARS2 is essential for the decay of both reporters and consistently co-immunoprecipitation analyses reveal a necessity of this domain for the interaction of ARS2 with the PAXT-associated RNA helicase MTR4. Taken together, our results map the domains of ARS2 underlying two essential properties of the protein: its RNP targeting ability and its capacity to recruit the RNA decay machinery.
UR - http://www.scopus.com/inward/record.url?scp=85088211365&partnerID=8YFLogxK
U2 - 10.1093/nar/gkaa445
DO - 10.1093/nar/gkaa445
M3 - Journal article
C2 - 32463452
AN - SCOPUS:85088211365
SN - 0305-1048
VL - 48
SP - 6943
EP - 6953
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - 12
ER -