ArticleNucleic acids research1994
Binding of Y-box proteins to RNA: involvement of different protein domains.
Article in Nucleic acids research, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 73 citations in OpenAlex.
- Y-box binding proteins in immunity and RNA virus infection.Microbiology and molecular biology reviews : MMBR · 2025Review
- The autophagy initiation factor ATG13 mRNA is stabilized by the RNA-binding protein YBX3.FEBS letters · 2025Article
- Ewing Sarcoma Related protein 1 recognizes R-loops by binding DNA forks.Biopolymers · 2024Article
- Genomic basis of environmental adaptation in the leathery sea squirt (Styela clava).Molecular ecology resources · 2020Article
- Y-Box Binding Proteins in mRNP Assembly, Translation, and Stability Control.Biomolecules · 2020Review
- The role of cold shock domain proteins in inflammatory diseases.Journal of molecular medicine (Berlin, Germany) · 2014Review
- BORIS/CTCFL is an RNA-binding protein that associates with polysomes.BMC cell biology · 2013Article
- Cold shock Y-box protein-1 proteolysis autoregulates its transcriptional activities.Cell communication and signaling : CCS · 2013Article
- A conserved stem loop motif in the 5'untranslated region regulates transforming growth factor-β(1) translation.PloS one · 2010Article
- An acidic protein, YBAP1, mediates the release of YB-1 from mRNA and relieves the translational repression activity of YB-1.Molecular and cellular biology · 2005Article
- Characterization of the 5'-untranslated region of YB-1 mRNA and autoregulation of translation by YB-1 protein.Nucleic acids research · 2004Article
- Thrombin induces the release of the Y-box protein dbpB from mRNA: a mechanism of transcriptional activation.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Y box-binding protein-1 binds preferentially to single-stranded nucleic acids and exhibits 3'-->5' exonuclease activity.Nucleic acids research · 2001Article
- Chicken Y-box proteins chk-YB-1b and chk-YB-2 repress translation by sequence-specific interaction with single-stranded RNA.The Biochemical journal · 2000Article
- Scp160p, a multiple KH-domain protein, is a component of mRNP complexes in yeast.Nucleic acids research · 2000Article
- Characterization of the DNA-binding domain of the avian Y-box protein, chkYB-2, and mutational analysis of its single-strand binding motif in the Rous sarcoma virus enhancer.Journal of virology · 1998Article
- Identification and developmental characterization of a novel Y-box protein from Drosophila melanogaster.Nucleic acids research · 1997Article
- Xp54, the Xenopus homologue of human RNA helicase p54, is an integral component of stored mRNP particles in oocytes.Nucleic acids research · 1997Article
- Y-box proteins interact with the S1 nuclease-sensitive site in the chicken alpha 2(I) collagen gene promoter.The Biochemical journal · 1996Article
- Review
Corrections and comments
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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
Eukaryotic Y-box proteins are reported to interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins. The modular structure of Y-box proteins includes a highly conserved N-terminal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) plus four basic C-terminal domains containing arginine clusters and aromatic residues. In addition, the basic domains are separated by acidic regions which contain several potential sites for serine/threonine phosphorylation. The interaction of Y-box proteins, isolated from Xenopus oocytes (FRGY2 type), with RNA molecules has been studied by UV crosslinking and protein fragmentation. We have identified two distinct binding activities. The CSD interacts preferentially with the polypurines poly(A,G) and poly(G) but not poly(A), this activity being sensitive to 5 mM MgCl2 but not to 5 mM spermidine. In the presence of 1 mM MgCl2 or 1 mM spermidine, the basic domains interact preferentially with poly(C,U), this activity being sensitive to 0.5 M NaCl. Binding of the basic domains is also sensitive to low concentrations of heparin. The basic domains can be crosslinked individually to labelled RNA. These results are discussed with reference to the various specificities noted in the binding of Y-box proteins to RNA and DNA.
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