ArticleRNA (New York, N.Y.)2005
Conformation of 4.5S RNA in the signal recognition particle and on the 30S ribosomal subunit.
Article in RNA (New York, N.Y.), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 30 citations in OpenAlex.
- The Nucleic Acids Circular Dichroism and Fourier Transform Databases NACDDB and NAIRDB: New Tools for RNA Structural Analysis.Methods in molecular biology (Clifton, N.J.) · 2026Article
- A production platform for disulfide-bonded peptides in the periplasm of Escherichia coli.Microbial cell factories · 2024Article
- Bacterial Small RNAs in the GenusInternational journal of molecular sciences · 2018Article
- Polynucleotide Phosphorylase, RNase E/G, and YbeY Are Involved in the Maturation of 4.5S RNA in Corynebacterium glutamicum.Journal of bacteriology · 2017Article
- Ribosome-associated ncRNAs: an emerging class of translation regulators.RNA biology · 2014Article
- Strong anion-exchange fast performance liquid chromatography as a versatile tool for preparation and purification of RNA produced by in vitro transcription.RNA (New York, N.Y.) · 2013Article
- Unraveling the dynamics of ribosome translocation.Current opinion in structural biology · 2012Review
- A genomic-library based discovery of a novel, possibly synthetic, acid-tolerance mechanism in Clostridium acetobutylicum involving non-coding RNAs and ribosomal RNA processing.Metabolic engineering · 2010Article
- Conformation of the signal recognition particle in ribosomal targeting complexes.RNA (New York, N.Y.) · 2009Article
- Demonstration of a multistep mechanism for assembly of the SRP x SRP receptor complex: implications for the catalytic role of SRP RNA.Journal of molecular biology · 2008Article
- Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- SRP RNA provides the physiologically essential GTPase activation function in cotranslational protein targeting.RNA (New York, N.Y.) · 2007Article
Corrections and comments
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Authors and funding
7 authors at 6 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The signal recognition particle (SRP) from Escherichia coli consists of 4.5S RNA and protein Ffh. It is essential for targeting ribosomes that are translating integral membrane proteins to the translocation pore in the plasma membrane. Independently of Ffh, 4.5S RNA also interacts with elongation factor G (EF-G) and the 30S ribosomal subunit. Here we use a cross-linking approach to probe the conformation of 4.5S RNA in SRP and in the complex with the 30S ribosomal subunit and to map the binding site. The UV-activatable cross-linker p-azidophenacyl bromide (AzP) was attached to positions 1, 21, and 54 of wild-type or modified 4.5S RNA. In SRP, cross-links to Ffh were formed from AzP in all three positions in 4.5S RNA, indicating a strongly bent conformation in which the 5' end (position 1) and the tetraloop region (including position 54) of the molecule are close to one another and to Ffh. In ribosomal complexes of 4.5S RNA, AzP in both positions 1 and 54 formed cross-links to the 30S ribosomal subunit, independently of the presence of Ffh. The major cross-linking target on the ribosome was protein S7; minor cross-links were formed to S2, S18, and S21. There were no cross-links from 4.5S RNA to the 50S subunit, where the primary binding site of SRP is located close to the peptide exit. The functional role of 4.5S RNA binding to the 30S subunit is unclear, as the RNA had no effect on translation or tRNA translocation on the ribosome.
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