ArticleNucleic acids research1997
A highly conserved nucleotide in the Alu domain of SRP RNA mediates translation arrest through high affinity binding to SRP9/14.
Article in Nucleic acids research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
- Lysosomal RNA profiling reveals targeting of specific types of RNAs for degradation.bioRxiv : the preprint server for biology · 2025Article
- Alu RNA pseudoknot alterations influence SRP9/SRP14 association.RNA (New York, N.Y.) · 2025Article
- The role of SRP9/SRP14 in regulating Alu RNA.RNA biology · 2024Review
- Alu RNA fold links splicing with signal recognition particle proteins.Nucleic acids research · 2023Article
- Nuclear SRP9/SRP14 heterodimer transcriptionally regulates 7SL and BC200 RNA expression.RNA (New York, N.Y.) · 2023Article
- Mouse germ line mutations due to retrotransposon insertions.Mobile DNA · 2019Review
- cis-Acting determinants of 7SL RNA packaging by HIV-1.Journal of virology · 2012Article
- Residues in SRP9/14 essential for elongation arrest activity of the signal recognition particle define a positively charged functional domain on one side of the protein.RNA (New York, N.Y.) · 2010Article
- Protein transport across and into cell membranes in bacteria and archaea.Cellular and molecular life sciences : CMLS · 2010Review
- Active Alu retrotransposons in the human genome.Genome research · 2008Article
- Anti-cooperative assembly of the SRP19 and SRP68/72 components of the signal recognition particle.The Biochemical journal · 2008Article
- Conserved tertiary base pairing ensures proper RNA folding and efficient assembly of the signal recognition particle Alu domain.Nucleic acids research · 2004Article
- Getting on target: the archaeal signal recognition particle.Archaea (Vancouver, B.C.) · 2002Article
- Evidence for a novel GTPase priming step in the SRP protein targeting pathway.The EMBO journal · 2001Article
- Elongation arrest is a physiologically important function of signal recognition particle.The EMBO journal · 2000Article
- Signal recognition particle components in the nucleolus.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure.RNA (New York, N.Y.) · 1999Article
- Localization of signal recognition particle RNA in the nucleolus of mammalian cells.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Binding of the signal recognition particle (SRP) to signal sequences during translation leads to an inhibition of polypeptide elongation known as translation arrest. The arrest activity is mediated by a discrete domain comprised of the Alu portion of SRP RNA and a 9 and 14 kDa polypeptide heterodimer (SRP9/14). Although very few nucleotides in SRP RNA are conserved throughout evolution, the remarkable conservation of G24, which resides in the region of SRP9/14 interaction, suggests that it is essential for translation arrest. To understand the functional significance of the G24 residue, we made single base substitutions in SRP RNA at this position and analyzed the ability of the mutants to bind SRP9/14 and to reconstitute functional SRPs. Mutation of G24 to C reduced binding to SRP9/14 by at least 50-fold, whereas mutation to A and U reduced binding approximately 2- and 5-fold respectively. The mutant RNAs could nevertheless assemble into SRPs at high subunit concentrations. SRPs reconstituted with mutant RNAs were not significantly defective in translation arrest assays, indicating that the conserved guanosine does not interact directly with the translational machinery. Taken together, these results demonstrate that G24 plays an important role in the translation arrest function of SRP by mediating high affinity binding of SRP9/14.
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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.