Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA

Yoichi Suzuki; Yoko Aoki; Yoshinori Ishida; Yasushi Chiba; Akihiro Iwamatsu; Tatsuya Kishino; Norio Niikawa; Yoichi Matsubara; Kuniaki Narisawa

doi:10.1038/ng1094-122

Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA

Yoichi Suzuki, Yoko Aoki, Yoshinori Ishida, Yasushi Chiba, Akihiro Iwamatsu, Tatsuya Kishino, Norio Niikawa, Yoichi Matsubara, Kuniaki Narisawa

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62 Citations (Scopus)

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.

Original language	English
Pages (from-to)	122-128
Number of pages	7
Journal	Nature Genetics
Volume	8
Issue number	2
DOIs	https://doi.org/10.1038/ng1094-122
Publication status	Published - 1994 Oct

ASJC Scopus subject areas

Genetics

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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.",

author = "Yoichi Suzuki and Yoko Aoki and Yoshinori Ishida and Yasushi Chiba and Akihiro Iwamatsu and Tatsuya Kishino and Norio Niikawa and Yoichi Matsubara and Kuniaki Narisawa",

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AU - Suzuki, Yoichi

AU - Aoki, Yoko

AU - Ishida, Yoshinori

AU - Chiba, Yasushi

AU - Iwamatsu, Akihiro

AU - Kishino, Tatsuya

AU - Niikawa, Norio

AU - Matsubara, Yoichi

AU - Narisawa, Kuniaki

PY - 1994/10

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N2 - 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.

AB - 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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Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA

Abstract

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