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- Title
Successful Conversion of the <i>Bacillus subtilis</i> BirA Group II Biotin Protein Ligase into a Group I Ligase.
- Authors
Henke, Sarah K.; Cronan, John E.
- 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.
- Subjects
BACILLUS subtilis; BIOTIN; LIGASES; TRANSCRIPTION factors; DNA-binding proteins; N-terminal residues
- Publication
PLoS ONE, 2014, Vol 9, Issue 5, p1
- ISSN
1932-6203
- Publication type
Article
- DOI
10.1371/journal.pone.0096757