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TitlePSRP1 is not a ribosomal protein, but a ribosome-binding factor that is recycled by the ribosome-recycling factor (RRF) and elongation factor G (EF-G).
Journal, issue, pagesJ Biol Chem, Vol. 285, Issue 6, Page 4006-4014, Year 2010
Publish dateFeb 5, 2010
AuthorsManjuli R Sharma / Alexandra Dönhöfer / Chandana Barat / Viter Marquez / Partha P Datta / Paola Fucini / Daniel N Wilson / Rajendra K Agrawal /
PubMed AbstractPlastid-specific ribosomal proteins (PSRPs) have been proposed to play roles in the light-dependent regulation of chloroplast translation. Here we demonstrate that PSRP1 is not a bona fide ribosomal ...Plastid-specific ribosomal proteins (PSRPs) have been proposed to play roles in the light-dependent regulation of chloroplast translation. Here we demonstrate that PSRP1 is not a bona fide ribosomal protein, but rather a functional homologue of the Escherichia coli cold-shock protein pY. Three-dimensional Cryo-electron microscopic (Cryo-EM) reconstructions reveal that, like pY, PSRP1 binds within the intersubunit space of the 70S ribosome, at a site overlapping the positions of mRNA and A- and P-site tRNAs. PSRP1 induces conformational changes within ribosomal components that comprise several intersubunit bridges, including bridge B2a, thereby stabilizes the ribosome against dissociation. We find that the presence of PSRP1/pY lowers the binding of tRNA to the ribosome. Furthermore, similarly to tRNAs, PSRP1/pY is recycled from the ribosome by the concerted action of the ribosome-recycling factor (RRF) and elongation factor G (EF-G). These results suggest a novel function for EF-G and RRF in the post-stress return of PSRP1/pY-inactivated ribosomes to the actively translating pool.
External linksJ Biol Chem / PubMed:19965869 / PubMed Central
MethodsEM (single particle)
Resolution9.8 - 14.1 Å
Structure data

EMDB-5125:
PSRP1 is not a bona fide ribosomal protein, but a stress response factor
Method: EM (single particle) / Resolution: 9.8 Å

EMDB-5126:
In vivo 70S E.coli ribosome with PSRP1
Method: EM (single particle) / Resolution: 14.1 Å

Source
  • Escherichia coli (E. coli)
  • Spinacia oleracea (spinach)

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