Gene cluster for dissimilatory nitrite reductase (nir) from Pseudomonas aeruginosa: Sequencing and identification of a locus for heme d(1) biosynthesis
Gene cluster for dissimilatory nitrite reductase (nir) from Pseudomonas aeruginosa: Sequencing and identification of a locus for heme d(1) biosynthesis
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DOI：
10.1128/jb.179.1.235-242.1997
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发表时间：
1997-01-01
影响因子：
3.2
通讯作者：
Igarashi, Y
中科院分区：
文献类型：
--
作者：
Kawasaki, S;Arai, H;Igarashi, Y
从铜绿假单胞菌中确定了产生活性异化亚硝酸盐还原酶所必需的nir基因簇的一级结构。从nirS到nirN，nirSMCF基因的终止密码子与nest基因的起始密码子紧密相连，表明nirSMCFDLGHJEN由一个调控nirSM转录的启动子表达。从nirDLGH基因推导的氨基酸序列彼此同源，命名为nirJ的编码387个氨基酸的蛋白质的基因显示出与每个nirDLGH基因的部分同一性，nirE基因编码与S-腺苷-L-甲硫氨酸同源的279个氨基酸的蛋白质：此外，NirE在N-末端100个氨基酸残基中与NirF显示21.0%的同一性，A基因，命名为nirN，编码493个氨基酸的蛋白质，具有保守的血红素c结合基序（CXXCH）和典型的N端膜转运信号序列。克隆的NirN蛋白与亚硝酸盐还原酶（NirS）的同源性为23.9%。插入突变和互补分析表明，nirFDLGHJE基因均为血红素d（1）生物合成所必需。
The primary structure of an nir gene cluster necessary for production of active dissimilatory nitrite reductase was determined from Pseudomonas aeruginosa. Seven open reading frames, designated nirDLGHJEN, were identified downstream of the previously reported nirSMCF genes, From nirS through nirN, the stop codon of one gene and the start codon of the nest gene were closely linked, suggesting that nirSMCFDLGHJEN are expressed from a promoter which regulates the transcription of nirSM. The amino acid sequences deduced from the nirDLGH genes were homologous to each other, A gene, designated nirJ, which encodes a protein of 387 amino acids, showed partial identity with each of the nirDLGH genes, The nirE gene encodes a protein of 279 amino acids homologous to S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase from other bacterial strains, In addition, NirE shows 21.0% identity with NirF in the N-terminal 100-amino-acid residues, A gene, designated nirN, encodes a protein of 493 amino acids with a conserved binding motif for heme c (CXXCH) and a typical N-terminal signal sequence for membrane translocation. The derived NirN protein shows 23.9% identity with nitrite reductase (NirS), Insertional mutation and complementation analyses showed that all of the nirFDLGHJE genes were necessary for the biosynthesis of heme d(1).