ArticleProtein science : a publication of the Protein Society2006
Protein SRP68 of human signal recognition particle: identification of the RNA and SRP72 binding domains.
Article in Protein science : a publication of the Protein Society, 2006. 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, 19 citations in OpenAlex.
- Cryo-EM structure of SRP68/72 reveals an extended dimerization domain with RNA-binding activity.Nucleic acids research · 2024Article
- The role of SRP9/SRP14 in regulating Alu RNA.RNA biology · 2024Review
- Proteomic-Based Machine Learning Analysis Reveals PYGB as a Novel Immunohistochemical Biomarker to Distinguish Inverted Urothelial Papilloma From Low-Grade Papillary Urothelial Carcinoma With Inverted Growth.Frontiers in oncology · 2022Article
- Human apo-SRP72 and SRP68/72 complex structures reveal the molecular basis of protein translocation.Journal of molecular cell biology · 2017Article
- Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction.Nucleic acids research · 2017Article
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
- A novel histone H4 arginine 3 methylation-sensitive histone H4 binding activity and transcriptional regulatory function for signal recognition particle subunits SRP68 and SRP72.The Journal of biological chemistry · 2012Article
- Article
- Identification of amino acid residues in protein SRP72 required for binding to a kinked 5e motif of the human signal recognition particle RNA.BMC molecular biology · 2010Article
- Characterization of the SRP68/72 interface of human signal recognition particle by systematic site-directed mutagenesis.Protein science : a publication of the Protein Society · 2009Article
- Anti-cooperative assembly of the SRP19 and SRP68/72 components of the signal recognition particle.The Biochemical journal · 2008Article
- The 5e motif of eukaryotic signal recognition particle RNA contains a conserved adenosine for the binding of SRP72.RNA (New York, N.Y.) · 2008Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The signal recognition particle (SRP) plays an important role in the delivery of secretory proteins to cellular membranes. Mammalian SRP is composed of six polypeptides among which SRP68 and SRP72 form a heterodimer that has been notoriously difficult to investigate. Human SRP68 was purified from overexpressing Escherichia coli cells and was found to bind to recombinant SRP72 as well as in vitro-transcribed human SRP RNA. Polypeptide fragments covering essentially the entire SRP68 molecule were generated recombinantly or by proteolytic digestion. The RNA binding domain of SRP68 included residues from positions 52 to 252. Ninety-four amino acids near the C terminus of SRP68 mediated the binding to SRP72. The SRP68-SRP72 interaction remained stable at elevated salt concentrations and engaged approximately 150 amino acids from the N-terminal region of SRP72. This portion of SRP72 was located within a predicted tandem array of four tetratricopeptide (TPR)-like motifs suggested to form a superhelical structure with a groove to accommodate the C-terminal region of SRP68.
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Registered trials
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.