Disease relevance of birA

• We isolated 21 human HCS cDNA clones, in four size classes of 2.0-4.0 kb, by complementation of an Escherichia coli birA mutant defective in biotin ligase [1].
• The Bacillus subtilis birA gene, which regulates biotin biosynthesis, has been cloned and characterized [2].

High impact information on birA

• We now report that a BCCP-87 species to which the biotin moiety was attached by chemical acylation rather than by biotin protein ligase showed the characteristically greater stability of the holo biotinoyl domain [3].
• Biotinylation in vivo is an extremely selective post-translational event where the enzyme biotin protein ligase (BPL) catalyzes the covalent attachment of biotin to one specific and conserved lysine residue of biotin-dependent enzymes [4].
• Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase [5].
• We have used localized mutagenesis of the biotin domain of the Escherichia coli biotin carboxyl carrier protein coupled with a genetic selection to identify regions of the domain having a role in interactions with the modifying enzyme, biotin protein ligase [5].
• The bifunctional birA gene product, BirA, which represses the biotin biosynthetic bio operon and also activates biotin in Escherichia coli, has been crystallized [6].

Biological context of birA

• First, birA plasmids complemented birA mutants for both the repressor and biotin holoenzyme synthetase activities of BirA [7].
• The birA gene maps at 202 degrees on the B. subtilis chromosome and encodes a 36,200-Da protein that is 27% identical to Escherichia coli BirA protein [2].
• Nucleotide sequence analysis of 18 mutations in the birA gene was employed to study the DNA-binding and enzymatic functions of the BirA protein [8].
• 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 [9].
• The protein was found to fall into the alpha/beta class and to be structurally homologous to the catalytic domains of class II aminoacyl-tRNA synthases and biotin protein ligase, BirA [10].

Associations of birA with chemical compounds

• For the several birA mutants examined, there appeared to be no direct correlation between effects on minimum biotin requirement and alterations in repressibility, suggesting a possible dual function for the gene [11].
• The birA protein has been purified to homogeneity in a three-step process involving chromatography on phosphocellulose and hydroxyapatite columns [7].
• BCCP becomes an active substrate for carboxylation and carboxyl transfer, after biotinylation of its canonical lysine residue by biotin protein ligase (BPL) [12].

References