ArticleThe Journal of cell biology1997
Xlrbpa, a double-stranded RNA-binding protein associated with ribosomes and heterogeneous nuclear RNPs.
Article in The Journal of cell biology, 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, 62 citations in OpenAlex.
- Article
- Compaction of RNA Duplexes in the Cell*.Angewandte Chemie (International ed. in English) · 2020Article
- Structural basis of siRNA recognition by TRBP double-stranded RNA binding domains.The EMBO journal · 2018Article
- Gemin5: A Multitasking RNA-Binding Protein Involved in Translation Control.Biomolecules · 2015Review
- Review
- The rough endoplasmatic reticulum is a central nucleation site of siRNA-mediated RNA silencing.The EMBO journal · 2013Article
- RNA aptamers binding the double-stranded RNA-binding domain.RNA (New York, N.Y.) · 2006Article
- Processing of pre-microRNAs by the Dicer-1-Loquacious complex in Drosophila cells.PLoS biology · 2005Article
- The double-stranded-RNA-binding motif: interference and much more.Nature reviews. Molecular cell biology · 2004Review
- Bioinformatic analysis of the nucleolus.The Biochemical journal · 2003Review
- Modulation of RNA editing by functional nucleolar sequestration of ADAR2.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Molecular mapping of the determinants involved in human Staufen-ribosome association.The Biochemical journal · 2002Article
- Lampbrush chromosomes and associated bodies: new insights into principles of nuclear structure and function.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2002Review
- Association of human immunodeficiency virus type 1 Vif with RNA and its role in reverse transcription.Journal of virology · 2000Article
- A human sequence homologue of Staufen is an RNA-binding protein that is associated with polysomes and localizes to the rough endoplasmic reticulum.Molecular and cellular biology · 1999Article
- Mammalian staufen is a double-stranded-RNA- and tubulin-binding protein which localizes to the rough endoplasmic reticulum.Molecular and cellular biology · 1999Article
- The RNA-editing enzyme ADAR1 is localized to the nascent ribonucleoprotein matrix on Xenopus lampbrush chromosomes but specifically associates with an atypical loop.The Journal of cell biology · 1999Article
- Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA.The EMBO journal · 1998Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have cloned and characterized Xlrbpa, a double-stranded RNA-binding protein from Xenopus laevis. Xlrbpa is a protein of 33 kD and contains three tandemly arranged, double-stranded RNA-binding domains (dsRBDs) that bind exclusively to double-stranded RNA in vitro, but fail to bind either single-stranded RNA or DNA. Sequence data and the overall organization of the protein suggest that Xlrbpa is the Xenopus homologue of human TAR-RNA binding protein (TRBP), a protein isolated by its ability to bind to human immunodeficiency virus (HIV) TAR-RNA. In transfection assays, TRBP has also been shown to inhibit the interferon-induced protein kinase PKR possibly by direct physical interaction. To determine the function of Xlrbpa and its human homologue we studied the expression and intracellular distribution of the two proteins. Xlrbpa is ubiquitously expressed with marked quantitative differences amongst all tissues. Xlrbpa and human TRBP can be detected in the cytoplasm and nucleus by immunofluorescence staining and Western blotting. Sedimentation gradient analyses and immunoprecipitation experiments suggest an association of cytoplasmic Xlrbpa with ribosomes. In contrast, a control construct containing two dsRBDs fails to associate with ribosomes in microinjected Xenopus oocytes. Nuclear staining of Xenopus lampbrush chromosome preparations showed the association of the protein with nucleoli, again indicating an association of the protein with ribosomal RNAs. Additionally, Xlrbpa could be located on lampbrush chromosomes and in snurposomes. Immunoprecipitations of nuclear extracts demonstrated the presence of the protein in heterogeneous nuclear (hn) RNP particles, but not in small nuclear RNPs, explaining the chromosomal localization of the protein. It thus appears that Xlrbpa is a general double-stranded RNA-binding protein which is associated with the majority of cellular RNAs, ribosomal RNAs, and hnRNAs either alone or as part of an hnRNP complex.
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