Oliver Antonio, Sánchez Juan Manuel, Blázquez Jesús
Unidad de Microbiología Molecular, Servicio de Microbiología, Hospital Ramón y Cajal, Carretera de Colmenar Km 9.1, 28034, Madrid, Spain.
FEMS Microbiol Lett. 2002 Nov 19;217(1):31-5. doi: 10.1111/j.1574-6968.2002.tb11452.x.
The mutT, mutM, and mutY genes of the GO system of the Pseudomonas aeruginosa PAO1 strain have been characterized by cloning, sequencing, and complementation analysis. The three genes, when cloned in a plasmid, were able to complement the high mutation frequency of the corresponding Escherichia coli deficient strains. Our results demonstrate that the putative mutT, mutM, and mutY gene products from P. aeruginosa are able to perform the expected activity. In addition, the sequence of the P. aeruginosa mutT gene strongly suggested that the product of this gene has a bifunctional activity in P. aeruginosa, being the C-terminal part 40% identical to a consensus sequence of thiamine monophosphate synthases. Our results also demonstrated that the N-terminal part of the protein is necessary and sufficient for the 8-oxodGTP hydrolase activity.
通过克隆、测序和互补分析对铜绿假单胞菌PAO1菌株GO系统的mutT、mutM和mutY基因进行了表征。这三个基因克隆到质粒中时,能够互补相应大肠杆菌缺陷菌株的高突变频率。我们的结果表明,来自铜绿假单胞菌的推定mutT、mutM和mutY基因产物能够发挥预期的活性。此外,铜绿假单胞菌mutT基因的序列强烈表明,该基因的产物在铜绿假单胞菌中具有双功能活性,其C末端部分与硫胺单磷酸合酶的共有序列有40%的同一性。我们的结果还表明,该蛋白质的N末端部分对于8-氧代鸟嘌呤三磷酸水解酶活性是必要且充分的。