ArticleNucleic acids research2011
Prevention of cross-talk in conserved regulatory systems: identification of specificity determinants in RNA-binding anti-termination proteins of the BglG family.
Article in Nucleic acids research, 2011. 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, 17 citations in OpenAlex.
- Identification and regulation of an alternative PTS for disaccharide utilization inApplied and environmental microbiology · 2025Article
- Precise prediction of hotspot residues in protein-RNA complexes using graph attention networks and pretrained protein language models.Bioinformatics (Oxford, England) · 2025Article
- Regulatory RNAs inSynthetic and systems biotechnology · 2024Review
- An autoinhibitory mechanism controls RNA-binding activity of the nitrate-sensing protein NasR.Molecular microbiology · 2020Article
- Intermolecular Communication inFrontiers in molecular biosciences · 2020Review
- Posttranscription Initiation Control of Gene Expression Mediated by Bacterial RNA-Binding Proteins.Annual review of microbiology · 2019Review
- Competitive folding of RNA structures at a termination-antitermination site.RNA (New York, N.Y.) · 2017Article
- Regulatory RNAs in Bacillus subtilis: a Gram-Positive Perspective on Bacterial RNA-Mediated Regulation of Gene Expression.Microbiology and molecular biology reviews : MMBR · 2016Review
- Far from being well understood: multiple protein phosphorylation events control cell differentiation in Bacillus subtilis at different levels.Frontiers in microbiology · 2014Article
- Dynamic localization of a transcription factor in Bacillus subtilis: the LicT antiterminator relocalizes in response to inducer availability.Journal of bacteriology · 2013Article
- 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
- The UlaG protein family defines novel structural and functional motifs grafted on an ancient RNase fold.BMC evolutionary biology · 2011Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Each family of signal transduction systems requires specificity determinants that link individual signals to the correct regulatory output. In Bacillus subtilis, a family of four anti-terminator proteins controls the expression of genes for the utilisation of alternative sugars. These regulatory systems contain the anti-terminator proteins and a RNA structure, the RNA anti-terminator (RAT) that is bound by the anti-terminator proteins. We have studied three of these proteins (SacT, SacY, and LicT) to understand how they can transmit a specific signal in spite of their strong structural homology. A screen for random mutations that render SacT capable to bind a RNA structure recognized by LicT only revealed a substitution (P26S) at one of the few non-conserved residues that are in contact with the RNA. We have randomly modified this position in SacT together with another non-conserved RNA-contacting residue (Q31). Surprisingly, the mutant proteins could bind all RAT structures that are present in B. subtilis. In a complementary approach, reciprocal amino acid exchanges have been introduced in LicT and SacY at non-conserved positions of the RNA-binding site. This analysis revealed the key role of an arginine side-chain for both the high affinity and specificity of LicT for its cognate RAT. Introduction of this Arg at the equivalent position of SacY (A26) increased the RNA binding in vitro but also resulted in a relaxed specificity. Altogether our results suggest that this family of anti-termination proteins has evolved to reach a compromise between RNA binding efficacy and specific interaction with individual target sequences.
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