DISRUPTION OF THE GENE ENCODING THE NADH-BINDING SUBUNIT OF NADH-UBIQUINONE OXIDOREDUCTASE IN NEUROSPORA-CRASSA FORMATION OF A PARTIALLY ASSEMBLED ENZYME WITHOUT FMN AND THE IRON-SULFUR CLUSTER N-3

DISRUPTION OF THE GENE ENCODING THE NADH-BINDING SUBUNIT OF NADH-UBIQUINONE OXIDOREDUCTASE IN NEUROSPORA-CRASSA FORMATION OF A PARTIALLY ASSEMBLED ENZYME WITHOUT FMN AND THE IRON-SULFUR CLUSTER N-3
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DOI:
10.1111/j.1432-1033.1994.tb18655.x
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发表时间:
1994-03-01
期刊:
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子:
--
通讯作者:
WEISS, H
WEISS, H
中科院分区:
其他
文献类型:
--
作者:
FECKE, W;SLED, VD;WEISS, H

文献摘要

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在本研究中,粗神经孢子虫线粒体NADH的51-kDa NADH结合亚基:泛醌氧化还原酶(复合体I)的基因被同源替换为缺陷基因拷贝而失活。由此产生的突变体nuo51缺乏51-kDa亚基,没有复合物I活性,但仍以野生型生长速度的三分之一生长。替代NADH:泛醌氧化还原酶(s)的酶活性增加了两倍,而其他线粒体呼吸酶的活性正常。除了nadh结合亚基外,配合物I几乎完全组装,并且仍然具有epr可检测到的四个铁硫簇中的三个。由于缺失的亚基包含一个四核铁硫簇的序列基序,因此缺失的簇N-3被认为与该亚基结合。
In this study, the gene of the 51-kDa NADH-binding subunit of the mitochondrial NADH:ubiquinone oxidoreductase (complex I) in Neurospora crassa was inactivated by homologous replacement with a defective gene copy. The resulting mutant, nuo51, lacks the 51-kDa subunit and shows no complex I activity but still grows at one third of the wild-type growth rate. The enzyme activity of the alternative NADH:ubiquinone oxidoreductase(s) is increased twofold while the activities of the other mitochondrial respiratory enzymes are normal. Complex I is almost completely assembled except for the NADH-binding subunit and still possesses three out of the four EPR-detectable iron-sulphur clusters. Since the deleted subunit contains the sequence motif for one tetranuclear iron-sulphur cluster, the missing cluster N-3 is considered to be bound to this subunit.