ArticleThe EMBO journal1997
From genetic to structural characterization of a new class of RNA-binding domain within the SacY/BglG family of antiterminator proteins.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 76 citations in OpenAlex.
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- Live-cell RNA imaging with the inactivated endonuclease Csy4 enables new insights into plant virus transport through plasmodesmata.PLoS pathogens · 2025Article
- Posttranscription Initiation Control of Gene Expression Mediated by Bacterial RNA-Binding Proteins.Annual review of microbiology · 2019Review
- Characterization of D-Arabitol as Newly Discovered Carbon Source ofFrontiers in microbiology · 2019Article
- Cross Talk among Transporters of the Phosphoenolpyruvate-Dependent Phosphotransferase System in Bacillus subtilis.Journal of bacteriology · 2018Article
- Competitive folding of RNA structures at a termination-antitermination site.RNA (New York, N.Y.) · 2017Article
- Review
- RNA imaging in living cells - methods and applications.RNA biology · 2014Review
- Equivalence between Euler angle conventions for the description of tensorial interactions in liquid NMR: application to different software programs.Journal of biomolecular NMR · 2013Review
- Competitive folding of anti-terminator/terminator hairpins monitored by single molecule FRET.Nucleic acids research · 2013Article
- Determinants of interaction specificity of the Bacillus subtilis GlcT antitermination protein: functionality and phosphorylation specificity depend on the arrangement of the regulatory domains.The Journal of biological chemistry · 2012Article
- Structure of the RBD-PRDI fragment of the antiterminator protein GlcT.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Application of live-cell RNA imaging techniques to the study of retroviral RNA trafficking.Viruses · 2012Review
- Characterization of the Group A Streptococcus Mga virulence regulator reveals a role for the C-terminal region in oligomerization and transcriptional activation.Molecular microbiology · 2012Article
- Prevention of cross-talk in conserved regulatory systems: identification of specificity determinants in RNA-binding anti-termination proteins of the BglG family.Nucleic acids research · 2011Article
- Structural mechanism of signal transduction between the RNA-binding domain and the phosphotransferase system regulation domain of the LicT antiterminator.The Journal of biological chemistry · 2008Article
- How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria.Microbiology and molecular biology reviews : MMBR · 2006Review
- Keeping signals straight in transcription regulation: specificity determinants for the interaction of a family of conserved bacterial RNA-protein couples.Nucleic acids research · 2006Article
- Compartmentalization of gene expression during sporulation of Bacillus subtilis is compromised in mutants blocked at stage III of sporulation.Journal of bacteriology · 2004Article
- A protein-dependent riboswitch controlling ptsGHI operon expression in Bacillus subtilis: RNA structure rather than sequence provides interaction specificity.Nucleic acids research · 2004Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SacY is the prototype of a family of regulatory proteins able to prevent transcription termination. It interacts with a 29 nucleotide RNA sequence able to fold into a stem-loop structure and partially overlapping with a terminator sequence located in the 5' leader mRNA region of the gene it controls. We show here that the N-terminal fragment of SacY, SacY(1-55), and the corresponding fragments of other members of the family have antiterminator activities with efficiency and specificity identical to those of the full-length proteins. In vitro, this activity correlates with the specific affinity of SacY(1-55) for its RNA target. UV melting experiments demonstrate that SacY(1-55) binding stabilizes the RNA target structure. The NMR solution structure of SacY(1-55) is very similar to that obtained in the crystal (van Tilbeurgh et al., 1997): the peptide is folded as a symmetrical dimer without any structural homology with other RNA-binding domains yet characterized. According to a preliminary NMR analysis of the SacY(1-55)-RNA complex, the protein dimer is not disrupted upon RNA binding and several residues implicated in RNA recognition are located at the edge of the dimer interface. This suggests a new mode of protein-RNA interaction.
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