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TitleRibosome-NatA architecture reveals that rRNA expansion segments coordinate N-terminal acetylation.
Journal, issue, pagesNat Struct Mol Biol, Vol. 26, Issue 1, Page 35-39, Year 2019
Publish dateDec 17, 2018
AuthorsAlexandra G Knorr / Christian Schmidt / Petr Tesina / Otto Berninghausen / Thomas Becker / Birgitta Beatrix / Roland Beckmann /
PubMed AbstractThe majority of eukaryotic proteins are N-terminally α-acetylated by N-terminal acetyltransferases (NATs). Acetylation usually occurs co-translationally and defects have severe consequences. ...The majority of eukaryotic proteins are N-terminally α-acetylated by N-terminal acetyltransferases (NATs). Acetylation usually occurs co-translationally and defects have severe consequences. Nevertheless, it is unclear how these enzymes act in concert with the translating ribosome. Here, we report the structure of a native ribosome-NatA complex from Saccharomyces cerevisiae. NatA (comprising Naa10, Naa15 and Naa50) displays a unique mode of ribosome interaction by contacting eukaryotic-specific ribosomal RNA expansion segments in three out of four binding patches. Thereby, NatA is dynamically positioned directly underneath the ribosomal exit tunnel to facilitate modification of the emerging nascent peptide chain. Methionine amino peptidases, but not chaperones or signal recognition particle, would be able to bind concomitantly. This work assigns a function to the hitherto enigmatic ribosomal RNA expansion segments and provides mechanistic insights into co-translational protein maturation by N-terminal acetylation.
External linksNat Struct Mol Biol / PubMed:30559462
MethodsEM (single particle)
Resolution3.4 - 6.7 Å
Structure data

0201

6hd5

EMDB-0201, PDB-6hd5:
Cryo-EM structure of the ribosome-NatA complex
Method: EM (single particle) / Resolution: 4.8 Å

0202

6hd7

EMDB-0202, PDB-6hd7:
Cryo-EM structure of the ribosome-NatA complex
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-0203:
Cryo-EM structure of a RNaseI treated 80S ribosome
Method: EM (single particle) / Resolution: 6.7 Å

Chemicals

ChemComp-3HE:
4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}piperidine-2,6-dione

Source
  • Saccharomyces cerevisiae S288C (yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsTRANSLATION / N-terminal acetylation / protein modification / ribosome / expansion segments

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