作者: Brian W. Wortham , Marcos A. Oliveira , Jacqueline D. Fetherston , Robert D. Perry
DOI: 10.1111/J.1462-2920.2010.02219.X
关键词:
摘要: We previously showed that mutations in the genes encoding two main biosynthetic enzymes responsible for polyamine production, arginine decarboxylase (SpeA) and ornithine (SpeC) cause a loss of biofilm formation Yersinia pestis. In Y. pestis development is dependent on 6 Hms (hemin storage) proteins (HmsH, F, R, S, T P) grouped into 3 operons; hmsHFRS, hmsT hmsP. this article we show polyamines are necessary to maintain levels key proteins. absence there an approximately 93%, 43% 90% reduction protein HmsR, HmsS HmsT respectively. Overexpression hmsR from plasmids alone can restore SpeA(-)SpeC(-) mutant. Addition exogenous putrescine also restores normal HmsS, production. Analyses using transcriptional reporters quantitative RT-PCR indicate initiation transcription mRNA stability not reduced by deficiency. Instead, translational function at least part modulating translation HmsR HmsT. Although construction consensus Shine-Dalgarno sequence upstream modestly stimulation putrescine, additional mechanisms likely contribute polyamine-dependent expression Finally, have shown play role bubonic plague.