2. Academic Validation
  3. Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA

Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA

  • Nat Genet. 1994 Oct;8(2):122-8. doi: 10.1038/ng1094-122.
Y Suzuki 1,  Y Aoki,  Y Ishida,  Y Chiba,  A Iwamatsu,  T Kishino,  N Niikawa,  Y Matsubara,  K Narisawa
Affiliations

Affiliation

  • 1 Department of Biomedical Genetics, Tohoku University School of Medicine, Sendai, Japan.
PMID: 7842009 DOI: 10.1038/ng1094-122
Abstract

Holocarboxylase synthetase (HCS) plays an essential role in biotin utilization in eukaryotic cells and its deficiency causes biotin-responsive multiple carboxylase deficiency in humans. We have cloned the human HCS cDNA and show that antiserum against the recombinant protein immunoprecipitates human HCS. A one base deletion resulting in a premature termination and a missense mutation (Leu to Pro) were found in cells from siblings with HCS deficiency. Human HCS shows homology to BirA, which acts as both a biotin-[acetyl-CoA-carboxylase] ligase and a biotin repressor in E. coli, suggesting a functional relationship between the two proteins. The human HCS gene maps to chromosome 21q22.1.

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