ArticleThe EMBO journal2000
Crystal structure of ribosomal protein L4 shows RNA-binding sites for ribosome incorporation and feedback control of the S10 operon.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024Article
- Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024Review
- Proteomic and Phenotypic Studies of Mycoplasma pneumoniae Revealed Macrolide-Resistant Mutation (A2063G) Associated Changes in Protein Composition and Pathogenicity of Type I Strains.Microbiology spectrum · 2023Article
- Clusters of bacterial RNA polymerase are biomolecular condensates that assemble through liquid-liquid phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Posttranscriptional Regulation ofJournal of bacteriology · 2020Article
- The extended loops of ribosomal proteins uL4 and uL22 of Escherichia coli contribute to ribosome assembly and protein translation.Nucleic acids research · 2016Article
- Ribosome Protein L4 is essential for Epstein-Barr Virus Nuclear Antigen 1 function.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Deletion of L4 domains reveals insights into the importance of ribosomal protein extensions in eukaryotic ribosome assembly.RNA (New York, N.Y.) · 2014Article
- Protein disorder in plants: a view from the chloroplast.BMC plant biology · 2012Article
- The role of disordered ribosomal protein extensions in the early steps of eubacterial 50 S ribosomal subunit assembly.International journal of molecular sciences · 2009Review
- Structural and functional analysis of the E. coli NusB-S10 transcription antitermination complex.Molecular cell · 2008Article
- Structure and function of an RNase H domain at the heart of the spliceosome.The EMBO journal · 2008Article
- Frequency of development and associated physiological cost of azithromycin resistance in Chlamydia psittaci 6BC and C. trachomatis L2.Antimicrobial agents and chemotherapy · 2007Article
- Functional analysis of Saccharomyces cerevisiae ribosomal protein Rpl3p in ribosome synthesis.Nucleic acids research · 2007Article
- In vitro selection and characterization of resistance to macrolides and related antibiotics in Mycoplasma pneumoniae.Antimicrobial agents and chemotherapy · 2004Article
- The extended loops of ribosomal proteins L4 and L22 are not required for ribosome assembly or L4-mediated autogenous control.RNA (New York, N.Y.) · 2003Article
- RNA-structural mimicry in Escherichia coli ribosomal protein L4-dependent regulation of the S10 operon.The Journal of biological chemistry · 2003Article
- The N-acetyltransferase RimJ responds to environmental stimuli to repress pap fimbrial transcription in Escherichia coli.Journal of bacteriology · 2002Article
- Natively unfolded proteins: a point where biology waits for physics.Protein science : a publication of the Protein Society · 2002Review
- Diversity of ribosomal mutations conferring resistance to macrolides, clindamycin, streptogramin, and telithromycin in Streptococcus pneumoniae.Antimicrobial agents and chemotherapy · 2002Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosomal protein L4 resides near the peptidyl transferase center of the bacterial ribosome and may, together with rRNA and proteins L2 and L3, actively participate in the catalysis of peptide bond formation. Escherichia coli L4 is also an autogenous feedback regulator of transcription and translation of the 11 gene S10 operon. The crystal structure of L4 from Thermotoga maritima at 1.7 A resolution shows the protein with an alternating alpha/beta fold and a large disordered loop region. Two separate binding sites for RNA are discernible. The N-terminal site, responsible for binding to rRNA, consists of the disordered loop with flanking alpha-helices. The C-terminal site, a prime candidate for the interaction with the leader sequence of the S10 mRNA, involves two non-consecutive alpha-helices. The structure also suggests a C-terminal protein-binding interface, through which L4 could be interacting with protein components of the transcriptional and/or translational machineries.
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