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来自大肠杆菌的硒代半胱氨酸合酶。基因(selA)的核苷酸序列及蛋白质的纯化。

Selenocysteine synthase from Escherichia coli. Nucleotide sequence of the gene (selA) and purification of the protein.

作者信息

Forchhammer K, Leinfelder W, Boesmiller K, Veprek B, Böck A

机构信息

Lehrstuhl für Mikrobiologie, Universität München, Federal Republic of Germany.

出版信息

J Biol Chem. 1991 Apr 5;266(10):6318-23.

PMID:2007584
Abstract

The nucleotide sequence of the selA gene from Escherichia coli whose product is involved in the conversion of seryl-tRNA(Sec UCA) into selenocysteyl-tRNA(Sec UCA) was determined. selA codes for a polypeptide of a calculated Mr of 50,667; a protein of appropriate size was synthesized in vivo in a T7 promoter/polymerase system. An assay for SELA activity was devised which is based on the seryl-tRNA(Sec UCA)-dependent incorporation of [75Se] selenium into acid-insoluble material. It was used to follow SELA purification from cells that overproduced the protein from a phage T7 promoter plasmid. Purified native SELA protein migrates in gel filtration experiments with a native Mr of about 600,000. SELA contains 1 mol of bound pyridoxal 5-phosphate/mol of 50-kDa subunit. Evidence is presented that the overall conversion of seryl-tRNA(Sec UCA) to selenocysteyl-tRNA(Sec UCA) occurs at the SELA protein. SELA, therefore, has the function of a selenocysteine synthase.

摘要

测定了来自大肠杆菌的selA基因的核苷酸序列,其产物参与丝氨酰 - tRNA(Sec UCA)向硒代半胱氨酰 - tRNA(Sec UCA)的转化。selA编码一个计算分子量为50,667的多肽;在T7启动子/聚合酶系统中,体内合成了大小合适的蛋白质。设计了一种基于[75Se]硒依赖于丝氨酰 - tRNA(Sec UCA)掺入酸不溶性物质的SELA活性测定方法。它用于跟踪从噬菌体T7启动子质粒过量产生该蛋白质的细胞中SELA的纯化过程。纯化的天然SELA蛋白在凝胶过滤实验中以约600,000的天然分子量迁移。SELA每摩尔50 kDa亚基含有1摩尔结合的磷酸吡哆醛。有证据表明丝氨酰 - tRNA(Sec UCA)向硒代半胱氨酰 - tRNA(Sec UCA)的整体转化发生在SELA蛋白上。因此,SELA具有硒代半胱氨酸合酶的功能。

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