Kerby Robert L, Youn Hwan, Roberts Gary P
Department of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
J Bacteriol. 2008 May;190(9):3336-43. doi: 10.1128/JB.00033-08. Epub 2008 Mar 7.
Genomic analysis suggested the existence of a CO-sensing bacterial transcriptional regulator that couples an N-terminal PAS fold domain to a C-terminal DNA-binding LytTR domain. UV/visible-light spectral analyses of heterologously expressed, purified full-length proteins indicated that they contained a hexacoordinated b-type heme moiety that avidly binds CO and NO. Studies of protein variants strongly suggested that the PAS domain residues His74 and Met104 serve as the heme Fe(II) axial ligands, with displacement of Met104 upon binding of the gaseous effectors. Two RcoM (regulator of CO metabolism) homologs were shown to function in vivo as CO sensors capable of regulating an aerobic CO oxidation (cox) regulon. The genetic linkage of rcoM with both aerobic (cox) and anaerobic (coo) CO oxidation systems suggests that in different organisms RcoM proteins may control either regulon type.
基因组分析表明存在一种一氧化碳感应细菌转录调节因子,该因子将一个N端PAS折叠结构域与一个C端DNA结合LytTR结构域相连。对异源表达、纯化的全长蛋白进行紫外/可见光光谱分析表明,它们含有一个六配位b型血红素部分,该部分能强烈结合一氧化碳和一氧化氮。对蛋白变体的研究有力地表明,PAS结构域的His74和Met104残基作为血红素Fe(II)的轴向配体,气态效应物结合时Met104会被取代。两个RcoM(一氧化碳代谢调节因子)同源物在体内被证明可作为能够调节需氧一氧化碳氧化(cox)操纵子的一氧化碳传感器。rcoM与需氧(cox)和厌氧(coo)一氧化碳氧化系统的遗传联系表明,在不同生物体中,RcoM蛋白可能控制其中任何一种操纵子类型。