ArticleThe Journal of biological chemistry2010
PSRP1 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).
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 84 citations in OpenAlex.
- A conserved archaeal protein with evolutionary links to bacterial ribosome hibernation and eukaryotic energy sensing.The EMBO journal · 2026Article
- Ribosome hibernation in zinc-starvedMicrobiology spectrum · 2026Article
- Chloroplast-encoded small subunit extensions reshape the Chlamydomonas chlororibosome.Nature plants · 2026Article
- Plastid Engineering for Photosynthesis-Driven Synthesis of Hyaluronic Acid in Tobacco.Plant biotechnology journal · 2026Article
- Capturing ribosomal structures in cellular extracts with cryoPRISM: A purification-free cryoEM approach reveals novel structural states.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Chloroplast-encoded small subunit extensions reshape the Chlamydomonas chlororibosome.bioRxiv : the preprint server for biology · 2026Article
- Comparative organelle genome analysis of the sister genera Ceratocephala and Myosurus (Ranunculaceae) reveals fast evolutionary rates in arid and aquatic environments.BMC plant biology · 2025Article
- Changes in proteome and protein carbonylation in potato (Solanum tuberosum L.) under single and combined abiotic stresses.Scientific reports · 2025Article
- The PSRP2/4 Proteins Promote Viral Infection by Interacting with the VPg Protein of TuMV.Plants (Basel, Switzerland) · 2025Article
- Multifaceted roles of mycobacterial HflX: ribosome splitting, rRNA disordering, and drug resistance.Biochemical Society transactions · 2025Article
- Review
- Defining the heterogeneous composition of Arabidopsis thylakoid membrane.The Plant journal : for cell and molecular biology · 2025Article
- Mechanistic insights into the alternative ribosome recycling by HflXr.Nucleic acids research · 2024Article
- Cryo- EM structure of the mycobacterial 70S ribosome in complex with ribosome hibernation promotion factor RafH.Nature communications · 2024Article
- Rippling life on a dormant planet: hibernation of ribosomes, RNA polymerases, and other essential enzymes.Frontiers in microbiology · 2024Review
- Chloroplast gene expression: Recent advances and perspectives.Plant communications · 2023Review
- New perspectives on the molecular mechanisms of stress signalling by the nucleotide guanosine tetraphosphate (ppGpp), an emerging regulator of photosynthesis in plants and algae.The New phytologist · 2023Review
- Structure of Escherichia coli heat shock protein Hsp15 in complex with the ribosomal 50S subunit bearing peptidyl-tRNA.Nucleic acids research · 2022Article
- Stromal Protein Chloroplast Development and Biogenesis1 Is Essential for Chloroplast Development and Biogenesis inFrontiers in plant science · 2022Article
- Co-expression networks in Chlamydomonas reveal significant rhythmicity in batch cultures and empower gene function discovery.The Plant cell · 2021Article
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
Abstract
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.