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TitleMechanism of ribosome rescue by ArfA and RF2.
Journal, issue, pagesElife, Vol. 6, Year 2017
Publish dateMar 16, 2017
AuthorsGabriel Demo / Egor Svidritskiy / Rohini Madireddy / Ruben Diaz-Avalos / Timothy Grant / Nikolaus Grigorieff / Duncan Sousa / Andrei A Korostelev /
PubMed AbstractArfA rescues ribosomes stalled on truncated mRNAs by recruiting release factor RF2, which normally binds stop codons to catalyze peptide release. We report two 3.2 Å resolution cryo-EM structures - ...ArfA rescues ribosomes stalled on truncated mRNAs by recruiting release factor RF2, which normally binds stop codons to catalyze peptide release. We report two 3.2 Å resolution cryo-EM structures - determined from a single sample - of the 70S ribosome with ArfA•RF2 in the A site. In both states, the ArfA C-terminus occupies the mRNA tunnel downstream of the A site. One state contains a compact inactive RF2 conformation. Ordering of the ArfA N-terminus in the second state rearranges RF2 into an extended conformation that docks the catalytic GGQ motif into the peptidyl-transferase center. Our work thus reveals the structural dynamics of ribosome rescue. The structures demonstrate how ArfA 'senses' the vacant mRNA tunnel and activates RF2 to mediate peptide release without a stop codon, allowing stalled ribosomes to be recycled.
External linksElife / PubMed:28300532 / PubMed Central
MethodsEM (single particle)
Resolution3.2 Å
Structure data

8521

5u9f

EMDB-8521, PDB-5u9f:
3.2 A cryo-EM ArfA-RF2 ribosome rescue complex (Structure II)
Method: EM (single particle) / Resolution: 3.2 Å

8522

5u9g

EMDB-8522, PDB-5u9g:
3.2 A cryo-EM ArfA-RF2 ribosome rescue complex (Structure I)
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • escherichia coli (E. coli)
  • escherichia coli k-12 (bacteria)
KeywordsRIBOSOME / ARFA RF2 ribosome rescue complex

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