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Gene Review

birA  -  biotin--protein ligase

Escherichia coli O157:H7 str. EDL933

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Disease relevance of birA


High impact information on birA

  • To control protein-protein interactions with biotin, the biotin protein ligase BirA from E. coli was coexpressed in yeast with a streptavidin-LexA fusion protein and Avitag or BCCP biotin acceptor peptides fused to the B42 activation domain [2].
  • Recently certain mutants of the Escherichia coli biotin protein ligase have been shown to mediate "promiscuous" biotinylation of proteins [3].
  • Likewise, E. coli BCCP is not biotinylated by S. tokodaii BPL, indicating that the substrate specificity is different between the two organisms [4].
  • Oxaloacetate synthesis in the methanarchaeon Methanosarcina barkeri: pyruvate carboxylase genes and a putative Escherichia coli-type bifunctional biotin protein ligase gene (bpl/birA) exhibit a unique organization [5].
  • Analysis of a bioW-lacZ translational fusion indicated that expression of the biotin operon is regulated by biotin and the B. subtilis birA gene [6].

Chemical compound and disease context of birA


Biological context of birA

  • Secondly, we tested in vivo and in vitro site-directed biotinylation with two different tags, consisting of either 15 (AviTag) or 72 amino acids (BioEase tag), which serve as a substrate for bacterial biotin ligase birA [10].

Associations of birA with chemical compounds

  • We recently found that the substrate specificity of BPL from archaeon Sulfolobus tokodaii is totally different from those of many other organisms, in reflection of a difference in the local sequence of BCCP surrounding the canonical lysine residue [8].


  1. The biotin protein MadF of the malonate decarboxylase from Malonomonas rubra. Berg, M., Dimroth, P. Arch. Microbiol. (1998) [Pubmed]
  2. Control of gene expression with small molecules: biotin-mediated acylation of targeted lysine residues in recombinant yeast. Athavankar, S., Peterson, B.R. Chem. Biol. (2003) [Pubmed]
  3. Nonenzymatic biotinylation of a biotin carboxyl carrier protein: unusual reactivity of the physiological target lysine. Streaker, E.D., Beckett, D. Protein Sci. (2006) [Pubmed]
  4. A unique biotin carboxyl carrier protein in archaeon Sulfolobus tokodaii. Li, Y.Q., Sueda, S., Kondo, H., Kawarabayasi, Y. FEBS Lett. (2006) [Pubmed]
  5. Oxaloacetate synthesis in the methanarchaeon Methanosarcina barkeri: pyruvate carboxylase genes and a putative Escherichia coli-type bifunctional biotin protein ligase gene (bpl/birA) exhibit a unique organization. Mukhopadhyay, B., Purwantini, E., Kreder, C.L., Wolfe, R.S. J. Bacteriol. (2001) [Pubmed]
  6. Cloning, sequencing, and characterization of the Bacillus subtilis biotin biosynthetic operon. Bower, S., Perkins, J.B., Yocum, R.R., Howitt, C.L., Rahaim, P., Pero, J. J. Bacteriol. (1996) [Pubmed]
  7. Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis. Tozawa, K., Broadhurst, R.W., Raine, A.R., Fuller, C., Alvarez, A., Guillen, G., Padron, G., Perham, R.N. Eur. J. Biochem. (2001) [Pubmed]
  8. Substrate specificity of archaeon Sulfolobus tokodaii biotin protein ligase. Sueda, S., Li, Y.Q., Kondo, H., Kawarabayasi, Y. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  9. Targeted and proximity-dependent promiscuous protein biotinylation by a mutant Escherichia coli biotin protein ligase. Cronan, J.E. J. Nutr. Biochem. (2005) [Pubmed]
  10. Evaluation of two novel tag-based labelling technologies for site-specific modification of proteins. Tirat, A., Freuler, F., Stettler, T., Mayr, L.M., Leder, L. Int. J. Biol. Macromol. (2006) [Pubmed]
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