ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferon.
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ABSTRACT:
SUBMITTER: Patel JR
PROVIDER: S-EPMC3790048 | biostudies-literature | 2013 Sep
REPOSITORIES: biostudies-literature
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ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferon.
Patel Jenish R JR Jain Ankur A Chou Yi-ying YY Baum Alina A Ha Taekjip T García-Sastre Adolfo A
EMBO reports 20130712 9
The cytosolic pathogen sensor RIG-I is activated by RNAs with exposed 5'-triphosphate (5'-ppp) and terminal double-stranded structures, such as those that are generated during viral infection. RIG-I has been shown to translocate on dsRNA in an ATP-dependent manner. However, the precise role of the ATPase activity in RIG-I activation remains unclear. Using in vitro-transcribed Sendai virus defective interfering RNA as a model ligand, we show that RIG-I oligomerizes on 5'-ppp dsRNA in an ATP hydro ...[more]
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