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TitleLoss of a single methylation in 23S rRNA delays 50S assembly at multiple late stages and impairs translation initiation and elongation.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 117, Issue 27, Page 15609-15619, Year 2020
Publish dateJul 7, 2020
AuthorsWei Wang / Wanqiu Li / Xueliang Ge / Kaige Yan / Chandra Sekhar Mandava / Suparna Sanyal / Ning Gao /
PubMed AbstractRibosome biogenesis is a complex process, and dozens of factors are required to facilitate and regulate the subunit assembly in bacteria. The 2'-O-methylation of U2552 in 23S rRNA by ...Ribosome biogenesis is a complex process, and dozens of factors are required to facilitate and regulate the subunit assembly in bacteria. The 2'-O-methylation of U2552 in 23S rRNA by methyltransferase RrmJ is a crucial step in late-stage assembly of the 50S subunit. Its absence results in severe growth defect and marked accumulation of pre50S assembly intermediates. In the present work, we employed cryoelectron microscopy to characterize a set of late-stage pre50S particles isolated from an Δ strain. These assembly intermediates (solved at 3.2 to 3.8 Å resolution) define a collection of late-stage particles on a progressive assembly pathway. Apart from the absence of L16, L35, and L36, major structural differences between these intermediates and the mature 50S subunit are clustered near the peptidyl transferase center, such as H38, H68-71, and H89-93. In addition, the ribosomal A-loop of the mature 50S subunit from Δ strain displays large local flexibility on nucleotides next to unmethylated U2552. Fast kinetics-based biochemical assays demonstrate that the Δ 50S subunit is only 50% active and two times slower than the WT 50S subunit in rapid subunit association. While the Δ 70S ribosomes show no defect in peptide bond formation, peptide release, and ribosome recycling, they translocate with 20% slower rate than the WT ribosomes in each round of elongation. These defects amplify during synthesis of the full-length proteins and cause overall defect in protein synthesis. In conclusion, our data reveal the molecular roles of U2552 methylation in both ribosome biogenesis and protein translation.
External linksProc Natl Acad Sci U S A / PubMed:32571953 / PubMed Central
MethodsEM (single particle)
Resolution3.14 - 3.64 Å
Structure data

EMDB-30212:
State 3 of pre50SH ribosome from rrmj knock out E.coli strain
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-30213:
State 2 of pre50SH ribosome from RrmJ knock out E.coli stain
Method: EM (single particle) / Resolution: 3.26 Å

EMDB-30214:
State 1 of pre50SH ribosome from RrmJ knock out E.coli stain
Method: EM (single particle) / Resolution: 3.64 Å

30215

7bv8

EMDB-30215, PDB-7bv8:
Mature 50S ribosomal subunit from RrmJ knock out E.coli strain
Method: EM (single particle) / Resolution: 3.14 Å

Source
  • Escherichia coli (E. coli)
  • escherichia coli (strain k12) (bacteria)
KeywordsRIBOSOME / ribosome assembly / ribosome biogenesis

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