Isolation of a cDNA encoding human holocarboxylase synthetase by functional complementation of a biotin auxotroph of Escherichia coli.

@article{LenDelRo1995IsolationOA,
  title={Isolation of a cDNA encoding human holocarboxylase synthetase by functional complementation of a biotin auxotroph of Escherichia coli.},
  author={Alfonso Le{\'o}n-Del-R{\'i}o and Daniel Leclerc and Bj{\"o}rn {\AA}kerman and Nobuaki Wakamatsu and R. A. Gravel},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1995},
  volume={92 10},
  pages={4626-30}
}
Holocarboxylase synthetase (HCS) catalyzes the biotinylation of the four biotin-dependent carboxylases in human cells. Patients with HCS deficiency lack activity of all four carboxylases, indicating that a single HCS is targeted to the mitochondria and cytoplasm. 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. Expression of the cDNA clones promoted biotinylation of the bacterial biotinyl… CONTINUE READING