Pelzer Alexander, Polen Tino, Funken Horst, Rosenau Frank, Wilhelm Susanne, Bott Michael, Jaeger Karl-Erich
Institute of Molecular Enzyme Technology, Research Centre Juelich, Heinrich-Heine-University Duesseldorf, D-52426, Juelich, Germany.
Microbiologyopen. 2014 Feb;3(1):89-103. doi: 10.1002/mbo3.150. Epub 2013 Dec 26.
The open reading frame PA1242 in the genome of Pseudomonas aeruginosa PAO1 encodes a putative protease belonging to the peptidase S8 family of subtilases. The respective enzyme termed SprP consists of an N-terminal signal peptide and a so-called S8 domain linked by a domain of unknown function (DUF). Presumably, this DUF domain defines a discrete class of Pseudomonas proteins as homologous domains can be identified almost exclusively in proteins of the genus Pseudomonas. The sprP gene was expressed in Escherichia coli and proteolytic activity was demonstrated. A P. aeruginosa ∆sprP mutant was constructed and its gene expression pattern compared to the wild-type strain by genome microarray analysis revealing altered expression levels of 218 genes. Apparently, SprP is involved in regulation of a variety of different cellular processes in P. aeruginosa including pyoverdine synthesis, denitrification, the formation of cell aggregates, and of biofilms.
铜绿假单胞菌PAO1基因组中的开放阅读框PA1242编码一种假定的蛋白酶，属于枯草杆菌蛋白酶的肽酶S8家族。相应的酶称为SprP，由一个N端信号肽和一个通过未知功能域（DUF）连接的所谓S8结构域组成。据推测，这个DUF结构域定义了一类独特的假单胞菌蛋白，因为几乎只能在假单胞菌属的蛋白质中鉴定到同源结构域。sprP基因在大肠杆菌中表达，并证明了其蛋白水解活性。构建了铜绿假单胞菌∆sprP突变体，并通过基因组微阵列分析将其基因表达模式与野生型菌株进行比较，发现218个基因的表达水平发生了改变。显然，SprP参与了铜绿假单胞菌多种不同细胞过程的调控，包括绿脓菌素合成、反硝化作用、细胞聚集体形成和生物膜形成。
