ArticleThe EMBO journal1998
The crystal structure of ribosomal protein S4 reveals a two-domain molecule with an extensive RNA-binding surface: one domain shows structural homology to the ETS DNA-binding motif.
Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 73 citations in OpenAlex.
- Article
- 50S subunit recognition and modification by theProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Pseudouridine Synthase RsuA Captures an Assembly Intermediate that Is Stabilized by Ribosomal Protein S17.Biomolecules · 2020Article
- C6orf203 is an RNA-binding protein involved in mitochondrial protein synthesis.Nucleic acids research · 2019Article
- Quantitative proteomics revealed C6orf203/MTRES1 as a factor preventing stress-induced transcription deficiency in human mitochondria.Nucleic acids research · 2019Article
- Assembly constraints drive co-evolution among ribosomal constituents.Nucleic acids research · 2015Article
- Purification, crystallization and preliminary X-ray diffraction analysis of Imp3 in complex with an Mpp10 peptide involved in yeast ribosome biogenesis.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Specific contacts between protein S4 and ribosomal RNA are required at multiple stages of ribosome assembly.RNA (New York, N.Y.) · 2013Article
- Elucidation of motifs in ribosomal protein S9 that mediate its nucleolar localization and binding to NPM1/nucleophosmin.PloS one · 2012Article
- Slow formation of stable complexes during coincubation of minimal rRNA and ribosomal protein S4.Journal of molecular biology · 2011Article
- Global stabilization of rRNA structure by ribosomal proteins S4, S17, and S20.Journal of molecular biology · 2009Article
- Crystal structure of an RluF-RNA complex: a base-pair rearrangement is the key to selectivity of RluF for U2604 of the ribosome.Journal of molecular biology · 2009Article
- A minimized rRNA-binding site for ribosomal protein S4 and its implications for 30S assembly.Nucleic acids research · 2009Article
- RNA folding and ribosome assembly.Current opinion in chemical biology · 2008Review
- Ribosomal protein S9 is a novel B23/NPM-binding protein required for normal cell proliferation.The Journal of biological chemistry · 2008Article
- Assembly of the 5' and 3' minor domains of 16S ribosomal RNA as monitored by tethered probing from ribosomal protein S20.Journal of molecular biology · 2008Article
- Small but versatile: the extraordinary functional and structural diversity of the beta-grasp fold.Biology direct · 2007Article
- Temperature-dependent RNP conformational rearrangements: analysis of binary complexes of primary binding proteins with 16 S rRNA.Journal of molecular biology · 2007Article
- Structure of the pseudouridine synthase RsuA from Haemophilus influenzae.Acta crystallographica. Section F, Structural biology and crystallization communications · 2005Article
- Imp3p and Imp4p mediate formation of essential U3-precursor rRNA (pre-rRNA) duplexes, possibly to recruit the small subunit processome to the pre-rRNA.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
We report the 1.7 A crystal structure of ribosomal protein S4 from Bacillus stearothermophilus. To facilitate the crystallization, 41 apparently flexible residues at the N-terminus of the protein have been deleted (S4Delta41). S4Delta41 has two domains; domain 1 is completely alpha-helical and domain 2 comprises a five-stranded antiparallel beta-sheet with three alpha-helices packed on one side. Domain 2 is an insertion within domain 1, and it shows significant structural homology to the ETS domain of eukaryotic transcription factors. A phylogenetic analysis of the S4 primary structure shows that the likely RNA interaction surface is predominantly on one side of the protein. The surface is extensive and highly positively charged, and is centered on a distinctive canyon at the domain interface. The latter feature contains two arginines that are totally conserved in all known species of S4 including eukaryotes, and are probably crucial in binding RNA. As has been shown for other ribosomal proteins, mutations within S4 that affect ribosome function appear to disrupt the RNA-binding sites. The structure provides a framework with which to probe the RNA-binding properties of S4 by site-directed mutagenesis.
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