SuhB is a novel ribosome associated protein that regulates expression of MexXY by modulating ribosome stalling in Pseudomonas aeruginosa. Issue 2 (3rd August 2015)

• Record Type: Journal Article
• Authors: Shi, Jing; Jin, Yongxin; Bian, Ting; Li, Kewei; Sun, Ziyu; Cheng, Zhihui; Jin, Shouguang; Wu, Weihui
• Is Part Of: Molecular microbiology. Volume 98:Issue 2(2015)
• Page Start: 370
• Page End: 383
• Publication Date: 2015-08-03
• Subjects: Molecular microbiology -- Periodicals; 572.829
• DOI: 10.1111/mmi.13126
• Languages: English
• ISSNs: 0950-382X

Abstract

<abstract abstract-type="main"> <title>Summary</title> <p>Translation elongation is modulated by various ribosome‐binding proteins. Environmental stresses, such as starvation and antibiotics, can cause stalling of bacterial ribosomes, which may alter gene expression through a transcription or translation attenuation mechanism. In <italic>P</italic><italic>seudomonas aeruginosa</italic>, the expression of MexXY multidrug efflux system, which plays a significant role in resistance against aminoglycoside antibiotics, is controlled by a translation surveillance mechanism. Stalling of ribosome at the PA5471 leader peptide (PA5471.1) mRNA leads to transcription of PA5471, which subsequently up‐regulates the expression of MexXY. In this study, we found that mutation in a <italic>suh</italic><italic>B</italic> gene leads to decreased susceptibility to aminoglycosides. Transcriptomic analysis revealed an up‐regulation of MexXY and PA5471, which were demonstrated to be responsible for the decreased susceptibility of the <italic>suh</italic><italic>B</italic> mutant. We further demonstrated that PA5471.1 is essential for the up‐regulation of PA5471 in the <italic>suh</italic><italic>B</italic> mutant. Co‐immunoprecipitation assay revealed an interaction between SuhB and ribosome, suggesting a role of SuhB in translation. Indeed, higher amount of PA5471.1 mRNA was found to associate with ribosome isolated from the <italic>suh</italic><italic>B</italic> mutant, indicating increased ribosome stalling. Therefore, this study identified SuhB as a novel ribosome associated protein that is involved in modulating ribosome activity.</p> </abstract>