ArticlePloS one2014
Successful conversion of the Bacillus subtilis BirA Group II biotin protein ligase into a Group I ligase.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Pathway and protein channel engineering ofSynthetic and systems biotechnology · 2025Article
- TIE-UP-SIN: a novel method for enhanced identification of protein-protein interactions.Frontiers in microbiology · 2025Article
- Biotin protein ligase as you like it: Either extraordinarily specific or promiscuous protein biotinylation.Proteins · 2024Review
- The Classical, Yet Controversial, First Enzyme of Lipid Synthesis: Escherichia coli Acetyl-CoA Carboxylase.Microbiology and molecular biology reviews : MMBR · 2021Review
- A division of labor between two biotin protein ligase homologs.Molecular microbiology · 2021Article
- AirID, a novel proximity biotinylation enzyme, for analysis of protein-protein interactions.eLife · 2020Article
- Proximity Dependent Biotinylation: Key Enzymes and Adaptation to Proteomics Approaches.Molecular & cellular proteomics : MCP · 2020Review
- The Biotin Biosynthetic Pathway in Mycobacterium tuberculosis is a Validated Target for the Development of Antibacterial Agents.Current medicinal chemistry · 2020Review
- RNA-protein interaction detection in living cells.Nature methods · 2018Article
- A Canonical Biotin Synthesis Enzyme, 8-Amino-7-Oxononanoate Synthase (BioF), Utilizes Different Acyl Chain Donors in Bacillus subtilis and Escherichia coli.Applied and environmental microbiology · 2018Article
- A conserved regulatory mechanism in bifunctional biotin protein ligases.Protein science : a publication of the Protein Society · 2017Article
- Pimelic acid, the first precursor of the Bacillus subtilis biotin synthesis pathway, exists as the free acid and is assembled by fatty acid synthesis.Molecular microbiology · 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
- An improved smaller biotin ligase for BioID proximity labeling.Molecular biology of the cell · 2016Article
- Mechanisms of biotin-regulated gene expression in microbes.Synthetic and systems biotechnology · 2016Review
- A Biotin Biosynthesis Gene Restricted to Helicobacter.Scientific reports · 2016Article
- Paracoccus denitrificans possesses two BioR homologs having a role in regulation of biotin metabolism.MicrobiologyOpen · 2015Article
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Abstract
Group II biotin protein ligases (BPLs) are characterized by the presence of an N-terminal DNA binding domain that allows transcriptional regulation of biotin biosynthetic and transport genes whereas Group I BPLs lack this N-terminal domain. The Bacillus subtilis BPL, BirA, is classified as a Group II BPL based on sequence predictions of an N-terminal helix-turn-helix motif and mutational alteration of its regulatory properties. We report evidence that B. subtilis BirA is a Group II BPL that regulates transcription at three genomic sites: bioWAFDBI, yuiG and yhfUTS. Moreover, unlike the paradigm Group II BPL, E. coli BirA, the N-terminal DNA binding domain can be deleted from Bacillus subtilis BirA without adverse effects on its ligase function. This is the first example of successful conversion of a Group II BPL to a Group I BPL with retention of full ligase activity.
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