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TitleStructural analysis of RIG-I-like receptors reveals ancient rules of engagement between diverse RNA helicases and TRIM ubiquitin ligases.
Journal, issue, pagesMol Cell, Vol. 81, Issue 3, Page 599-613.e8, Year 2021
Publish dateFeb 4, 2021
AuthorsKazuki Kato / Sadeem Ahmad / Zixiang Zhu / Janet M Young / Xin Mu / Sehoon Park / Harmit S Malik / Sun Hur /
PubMed AbstractRNA helicases and E3 ubiquitin ligases mediate many critical functions in cells, but their actions have largely been studied in distinct biological contexts. Here, we uncover evolutionarily conserved ...RNA helicases and E3 ubiquitin ligases mediate many critical functions in cells, but their actions have largely been studied in distinct biological contexts. Here, we uncover evolutionarily conserved rules of engagement between RNA helicases and tripartite motif (TRIM) E3 ligases that lead to their functional coordination in vertebrate innate immunity. Using cryoelectron microscopy and biochemistry, we show that RIG-I-like receptors (RLRs), viral RNA receptors with helicase domains, interact with their cognate TRIM/TRIM-like E3 ligases through similar epitopes in the helicase domains. Their interactions are avidity driven, restricting the actions of TRIM/TRIM-like proteins and consequent immune activation to RLR multimers. Mass spectrometry and phylogeny-guided biochemical analyses further reveal that similar rules of engagement may apply to diverse RNA helicases and TRIM/TRIM-like proteins. Our analyses suggest not only conserved substrates for TRIM proteins but also, unexpectedly, deep evolutionary connections between TRIM proteins and RNA helicases, linking ubiquitin and RNA biology throughout animal evolution.
External linksMol Cell / PubMed:33373584 / PubMed Central
MethodsEM (single particle) / EM (helical sym.) / X-ray diffraction
Resolution1.92 - 4.3 Å
Structure data

22368

7jl0

EMDB-22368, PDB-7jl0:
Cryo-EM structure of MDA5-dsRNA in complex with TRIM65 PSpry domain (Monomer)
Method: EM (single particle) / Resolution: 4.3 Å

22369

7jl1

EMDB-22369, PDB-7jl1:
Cryo-EM structure of RIG-I:dsRNA in complex with RIPLET PrySpry domain (monomer)
Method: EM (single particle) / Resolution: 3.9 Å

22370

7jl2

EMDB-22370, PDB-7jl2:
Cryo-EM structure of MDA5-dsRNA filament in complex with TRIM65 PSpry domain (Trimer)
Method: EM (helical sym.) / Resolution: 4.3 Å

22371

7jl3

EMDB-22371, PDB-7jl3:
Cryo-EM structure of RIG-I:dsRNA filament in complex with RIPLET PrySpry domain (trimer)
Method: EM (helical sym.) / Resolution: 4.2 Å

PDB-7jl4:
Crystal structure of TRIM65 PSpry domain
Method: X-RAY DIFFRACTION / Resolution: 1.92 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-ALF:
TETRAFLUOROALUMINATE ION

ChemComp-MG:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE/IMMUNE SYSTEM/RNA / Innate immunity / Ubiquitin E3 ligase / dsRNA / RNA helicase / TRIM family / HYDROLASE-IMMUNE SYSTEM-RNA complex / HYDROLASE/TRANSFERASE/RNA / E3 ligase / helicase / antiviral signaling / RLR / dsRNA sensor / HYDROLASE-TRANSFERASE-RNA complex / ATPase / IMMUNE SYSTEM / RIG-I-like helicase

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