ArticleRNA (New York, N.Y.)1999
The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure.
Article in RNA (New York, N.Y.), 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- Alu RNA pseudoknot alterations influence SRP9/SRP14 association.RNA (New York, N.Y.) · 2025Article
- The RNA Helicase Ded1 from Yeast Is Associated with the Signal Recognition Particle and Is Regulated by SRP21.Molecules (Basel, Switzerland) · 2024Article
- The role of SRP9/SRP14 in regulating Alu RNA.RNA biology · 2024Review
- Noncanoncial signal recognition particle RNAs in a major eukaryotic phylum revealed by purification of SRP from the human pathogen Cryptococcus neoformans.Nucleic acids research · 2015Article
- Exportin-5 mediates nuclear export of SRP RNA in vertebrates.Genes to cells : devoted to molecular & cellular mechanisms · 2015Article
- Integrity of SRP RNA is ensured by La and the nuclear RNA quality control machinery.Nucleic acids research · 2014Article
- 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
- A nomenclature for all signal recognition particle RNAs.RNA (New York, N.Y.) · 2005Article
- Identification and comparative analysis of components from the signal recognition particle in protozoa and fungi.BMC genomics · 2004Article
- Saccharomyces SRP RNA secondary structures: a conserved S-domain and extended Alu-domain.RNA (New York, N.Y.) · 2004Article
- Prediction of signal recognition particle RNA genes.Nucleic acids research · 2002Article
- Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export.The Journal of cell biology · 2001Article
- Elongation arrest is a physiologically important function of signal recognition particle.The EMBO journal · 2000Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mammalian Alu domain of the signal recognition particle (SRP) consists of a heterodimeric protein SRP9/14 and the Alu portion of 7SL RNA and comprises the elongation arrest function of the particle. To define the domain in Saccharomyces cerevisiae SRP that is homologous to the mammalian Alu domain [Alu domain homolog in yeast (Adhy)], we examined the assembly of a yeast protein homologous to mammalian SRP14 (Srp14p) and scR1 RNA. Srp14p binds as a homodimeric complex to the 5' sequences of scR1 RNA. Its minimal binding site consists of 99 nt. (Adhy RNA), comprising a short hairpin structure followed by an extended stem. As in mammalian SRP9/14, the motif UGUAAU present in most SRP RNAs is part of the Srp14p binding sites as shown by footprint and mutagenesis studies. In addition, certain basic amino acid residues conserved between mammalian SRP14 and Srp14p are essential for RNA binding in both proteins. These findings confirm the common ancestry of the yeast and the mammalian components and indicate that Srp14p together with Adhy RNA represents the Alu domain homolog in yeast SRP that may comprise its elongation arrest function. Despite the similarities, Srp14p selectively recognizes only scR1 RNA, revealing substantial changes in RNA-protein recognition as well as in the overall structure of the complex. The alignment of the three yeast SRP RNAs known to date suggests a common structure for the putative elongation arrest domain of all three organisms.
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