ArticleThe Journal of biological chemistry2013
The wing of a winged helix-turn-helix transcription factor organizes the active site of BirA, a bifunctional repressor/ligase.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 25 citations in OpenAlex.
- Balanced Expression of the Diiron Oxygenase BioE Is Essential for Biotin Homeostasis in Elizabethkingia meningoseptica.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Biotin protein ligase as you like it: Either extraordinarily specific or promiscuous protein biotinylation.Proteins · 2024Review
- A division of labor between two biotin protein ligase homologs.Molecular microbiology · 2021Article
- XRE-Type Regulator BioX Acts as a Negative Transcriptional Factor of Biotin Metabolism in Riemerella anatipestifer.Journal of bacteriology · 2021Article
- Proximity Dependent Biotinylation: Key Enzymes and Adaptation to Proteomics Approaches.Molecular & cellular proteomics : MCP · 2020Review
- The nucleosome core particle remembers its position through DNA replication and RNA transcription.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- BioSITe: A Method for Direct Detection and Quantitation of Site-Specific Biotinylation.Journal of proteome research · 2018Article
- Abundance, diversity and domain architecture variability in prokaryotic DNA-binding transcription factors.PloS one · 2018Article
- Split-BioID a conditional proteomics approach to monitor the composition of spatiotemporally defined protein complexes.Nature communications · 2017Article
- The Staphylococcus aureus group II biotin protein ligase BirA is an effective regulator of biotin operon transcription and requires the DNA binding domain for full enzymatic activity.Molecular microbiology · 2016Article
- Functional definition of BirA suggests a biotin utilization pathway in the zoonotic pathogen Streptococcus suis.Scientific reports · 2016Article
- Deciphering a unique biotin scavenging pathway with redundant genes in the probiotic bacterium Lactococcus lactis.Scientific reports · 2016Article
- Mechanisms of biotin-regulated gene expression in microbes.Synthetic and systems biotechnology · 2016Review
- Article
- Successful conversion of the Bacillus subtilis BirA Group II biotin protein ligase into a Group I ligase.PloS one · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The BirA biotin protein ligase of Escherichia coli belongs to the winged helix-turn-helix (wHTH) family of transcriptional regulators. The N-terminal BirA domain is required for both transcriptional regulation of biotin synthesis and biotin protein ligase activity. We addressed the structural and functional role of the wing of the wHTH motif in both BirA functions. A panel of N-terminal deletion mutant proteins including a discrete deletion of the wing motif were unable to bind DNA. However, all the N-terminal deletion mutants weakly complemented growth of a ΔbirA strain at low biotin concentrations, indicating compromised ligase activity. A wing domain chimera was constructed by replacing the BirA wing with the nearly isosteric wing of the E. coli OmpR transcription factor. Although this chimera BirA was defective in operator binding, it was much more efficient in complementation of a ΔbirA strain than was the wing-less protein. The enzymatic activities of the wing deletion and chimera proteins in the in vitro synthesis of biotinoyl-5'-AMP differed greatly. The wing deletion BirA accumulated an off pathway compound, ADP, whereas the chimera protein did not. Finally, we report that a single residue alteration in the wing bypasses the deleterious effects caused by mutations in the biotin-binding loop of the ligase active site. We believe that the role of the wing in the BirA enzymatic reaction is to orient the active site and thereby protect biotinoyl-5'-AMP from attack by solvent. This is the first evidence that the wing domain of a wHTH protein can play an important role in enzymatic activity.
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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.