Human complex II(succinate-ubiquinone oxidoreductase): cDNA cloning of iron sulfur(Ip) subunit of liver mitochondria

Kiyoshi Kita; Hiroshi Oya; Robert B. Gennis; Brian A.C. Ackrell; Michihiro Kasahara

doi:10.1016/0006-291X(90)91916-G

Human complex II(succinate-ubiquinone oxidoreductase): cDNA cloning of iron sulfur(Ip) subunit of liver mitochondria

Kiyoshi Kita, Hiroshi Oya, Robert B. Gennis, Brian A.C. Ackrell, Michihiro Kasahara

Biochemistry

Research output: Contribution to journal › Article › peer-review

Abstract

Complex II (succinate-ubiquinone oxidoreductase) is an important enzyme complex of both the tricarboxylic acid cycle and of the aerobic respiratory chains of mitochondria in eukaryotic cell and prokaryotic organisms. In this study, the amino acid sequence of iron sulfur-subunit in human liver mitochondria was deduced from cDNA which was isolated by immunoscreening a human liver λ gtll cDNA library. An isolated clone contains an open reading frame of 786 nucleotides and encodes a mature potein of 252 amino acids with a molecular weight of 28,804. The amino acid sequence was highly homologous with that of bovine heart (94.1%) which has been determined from the purified peptide and that of Escherichia coli sdh B product (50.8%). Striking sequence conservation was found around the three cysteine-rich clusters which have been thought to comprise the iron-sulfur centers of the enzyme. This is the frrst report on the cDNA sequence of mitochondrial complex II.

Original language	English (US)
Pages (from-to)	101-108
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	166
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(90)91916-G
State	Published - Jan 15 1990

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(90)91916-G

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title = "Human complex II(succinate-ubiquinone oxidoreductase): cDNA cloning of iron sulfur(Ip) subunit of liver mitochondria",

abstract = "Complex II (succinate-ubiquinone oxidoreductase) is an important enzyme complex of both the tricarboxylic acid cycle and of the aerobic respiratory chains of mitochondria in eukaryotic cell and prokaryotic organisms. In this study, the amino acid sequence of iron sulfur-subunit in human liver mitochondria was deduced from cDNA which was isolated by immunoscreening a human liver λ gtll cDNA library. An isolated clone contains an open reading frame of 786 nucleotides and encodes a mature potein of 252 amino acids with a molecular weight of 28,804. The amino acid sequence was highly homologous with that of bovine heart (94.1%) which has been determined from the purified peptide and that of Escherichia coli sdh B product (50.8%). Striking sequence conservation was found around the three cysteine-rich clusters which have been thought to comprise the iron-sulfur centers of the enzyme. This is the frrst report on the cDNA sequence of mitochondrial complex II.",

author = "Kiyoshi Kita and Hiroshi Oya and Gennis, {Robert B.} and Ackrell, {Brian A.C.} and Michihiro Kasahara",

note = "Funding Information: Complex II (succinate-ubiouinone oxidoreductase) catalyzes the oxidation of succinate to fumarate (succinate dehydrogenase) and transfers its reducing equivalents to ubiquinone (see Refs. 1 and 2 for reviews). Complex II also catalyzes the reduction of fumarate, which is the reverse reaction catalyzed by succinate dehydrogenase, in the respiratory chain of tion, lThis work Science was and supported Culture by of Grant-in-Aid Japan (No. 01570142 from the and Ministry 01480173), of Educa-and by the grant from CIBA-GEIGY Foundation for the Promotion of Science, and by a grant from National Institute of Health (RBG), HL16101.",

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AU - Ackrell, Brian A.C.

AU - Kasahara, Michihiro

N1 - Funding Information: Complex II (succinate-ubiouinone oxidoreductase) catalyzes the oxidation of succinate to fumarate (succinate dehydrogenase) and transfers its reducing equivalents to ubiquinone (see Refs. 1 and 2 for reviews). Complex II also catalyzes the reduction of fumarate, which is the reverse reaction catalyzed by succinate dehydrogenase, in the respiratory chain of tion, lThis work Science was and supported Culture by of Grant-in-Aid Japan (No. 01570142 from the and Ministry 01480173), of Educa-and by the grant from CIBA-GEIGY Foundation for the Promotion of Science, and by a grant from National Institute of Health (RBG), HL16101.

PY - 1990/1/15

Y1 - 1990/1/15

N2 - Complex II (succinate-ubiquinone oxidoreductase) is an important enzyme complex of both the tricarboxylic acid cycle and of the aerobic respiratory chains of mitochondria in eukaryotic cell and prokaryotic organisms. In this study, the amino acid sequence of iron sulfur-subunit in human liver mitochondria was deduced from cDNA which was isolated by immunoscreening a human liver λ gtll cDNA library. An isolated clone contains an open reading frame of 786 nucleotides and encodes a mature potein of 252 amino acids with a molecular weight of 28,804. The amino acid sequence was highly homologous with that of bovine heart (94.1%) which has been determined from the purified peptide and that of Escherichia coli sdh B product (50.8%). Striking sequence conservation was found around the three cysteine-rich clusters which have been thought to comprise the iron-sulfur centers of the enzyme. This is the frrst report on the cDNA sequence of mitochondrial complex II.

AB - Complex II (succinate-ubiquinone oxidoreductase) is an important enzyme complex of both the tricarboxylic acid cycle and of the aerobic respiratory chains of mitochondria in eukaryotic cell and prokaryotic organisms. In this study, the amino acid sequence of iron sulfur-subunit in human liver mitochondria was deduced from cDNA which was isolated by immunoscreening a human liver λ gtll cDNA library. An isolated clone contains an open reading frame of 786 nucleotides and encodes a mature potein of 252 amino acids with a molecular weight of 28,804. The amino acid sequence was highly homologous with that of bovine heart (94.1%) which has been determined from the purified peptide and that of Escherichia coli sdh B product (50.8%). Striking sequence conservation was found around the three cysteine-rich clusters which have been thought to comprise the iron-sulfur centers of the enzyme. This is the frrst report on the cDNA sequence of mitochondrial complex II.

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Human complex II(succinate-ubiquinone oxidoreductase): cDNA cloning of iron sulfur(Ip) subunit of liver mitochondria

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