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Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA

Nature Genetics volume 8, pages 122–128 (1994)Cite this article

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 represser in E. coli, suggesting a functional relationship between the two proteins. The human HCS gene maps to chromosome 21q22.1.

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Authors and Affiliations

  1. Department of Biochemical Genetics, Tohoku University School of Medicine, Sendai, 980-77, Japan

    Yoichi Suzuki, Yoko Aoki, Yoshinori Ishida, Yasushi Chiba, Yoichi Matsubara & Kuniaki Narisawa

  2. Central Laboratories for Key Technology, Kirin Brewery Co., Ltd., Yokohama, 236, Japan

    Akihiro Iwamatsu

  3. Department of Human Genetics, Nagasaki University School of Medicine, Nagasaki, 852, Japan

    Tatsuya Kishino & Norio Niikawa

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Suzuki, Y., Aoki, Y., Ishida, Y. et al. Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA. Nat Genet 8, 122–128 (1994). https://doi.org/10.1038/ng1094-122

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