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

研究成果: Article › 査読

109 被引用数 (Scopus)

抄録

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.

本文言語	English
ページ（範囲）	122-128
ページ数	7
ジャーナル	Nature Genetics
巻	8
号	2
DOI	https://doi.org/10.1038/ng1094-122
出版ステータス	Published - 1994 10月

ASJC Scopus subject areas

遺伝学

文献へのアクセス

10.1038/ng1094-122

他のファイルとリンク

引用スタイル

@article{33b8b93b1d9a4d33843c522396f5e31f,

title = "Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA",

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",

year = "1994",

month = oct,

doi = "10.1038/ng1094-122",

language = "English",

volume = "8",

pages = "122--128",

journal = "Nature Genetics",

issn = "1061-4036",

publisher = "Nature Publishing Group",

number = "2",

}

TY - JOUR

T1 - Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA

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

Y1 - 1994/10

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.

UR - http://www.scopus.com/inward/record.url?scp=0027982429&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027982429&partnerID=8YFLogxK

U2 - 10.1038/ng1094-122

DO - 10.1038/ng1094-122

M3 - Article

C2 - 7842009

AN - SCOPUS:0027982429

VL - 8

SP - 122

EP - 128

JO - Nature Genetics

JF - Nature Genetics

SN - 1061-4036

IS - 2

ER -

Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA

抄録

ASJC Scopus subject areas

文献へのアクセス

他のファイルとリンク

フィンガープリント

引用スタイル