Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Gene Review:

birA - biotin--protein ligase

Escherichia coli CFT073

Tirat, A. et al., Rodionov, D.A. et al., Streaker, E.D. et al.

Rodionov, Mironov, Gelfand,

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Disease relevance of birA

When birA protein was co-expressed in E. coli biotin was incorporated almost completely into a model protein which carried these recognition tags at its C-terminus [1].

High impact information on birA

The strict control of biotin biosynthesis in Escherichia coli is mediated by the bifunctional BirA protein, which acts both as a biotin-protein ligase and as a transcriptional repressor of the biotin operon [2].
Recently certain mutants of the Escherichia coli biotin protein ligase have been shown to mediate "promiscuous" biotinylation of proteins [3].

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 [1].

References

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]
Conservation of the biotin regulon and the BirA regulatory signal in Eubacteria and Archaea. Rodionov, D.A., Mironov, A.A., Gelfand, M.S. Genome Res. (2002) [Pubmed]
Nonenzymatic biotinylation of a biotin carboxyl carrier protein: unusual reactivity of the physiological target lysine. Streaker, E.D., Beckett, D. Protein Sci. (2006) [Pubmed]

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