Successful conversion of the Bacillus subtilis BirA Group II biotin protein ligase into a Group I ligase.
Sarah K Henke, John E Cronan
文献索引:PLoS ONE 9(5) , e96757, (2014)
全文:HTML全文
摘要
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.
相关化合物
相关文献:
2014-01-01
[Retrovirology 11 , 118, (2015)]
2014-01-01
[PLoS ONE 9(9) , e108055, (2014)]
2014-07-07
[Mol. Pharm. 11(7) , 1991-6, (2014)]
2015-02-01
[Cancer Chemother. Pharmacol. 75(2) , 431-7, (2015)]
2015-02-15
[Food Chem. 169 , 28-33, (2014)]