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Functional replacement of the Escherichia coli hfq gene by the homologue of Pseudomonas aeruginosa

Institute of Microbiology and Genetics, Vienna Biocentre, Dr Bohrgasse 9, 1030 Vienna, Austria¹

Author for correspondence: Udo Bläsi. Tel: +43 1 4277 54609. Fax: +43 1 4277 9546. e-mail: udo.blaesi{at}univie.ac.at

The 102 aa Hfq protein of Escherichia coli (Hfq_Ec) was first described as a host factor required for phage Qß replication. More recently, Hfq was shown to affect the stability of several E. coli mRNAs, including ompA mRNA, where it interferes with ribosome binding, which in turn results in rapid degradation of the transcript. In contrast, Hfq is also required for efficient translation of the E. coli and Salmonella typhimurium rpoS gene, encoding the stationary factor. In this study, the authors have isolated and characterized the Hfq homologue of Pseudomonas aeruginosa (Hfq_Pa), which consists of only 82 aa. The 68 N-terminal amino acids of Hfq_Pa show 92% identity with Hfq_Ec. Hfq_Pa was shown to functionally replace Hfq_Ec in terms of its requirement for phage Qß replication and for rpoS expression. In addition, Hfq_Pa exerted the same negative effect on E. coli ompA mRNA expression. As judged by proteome analysis, the expression of either the plasmid-borne hfq_Pa or the hfq_Ec gene in an E. coli Hfq^- RpoS^- strain revealed no gross difference in the protein profile. Both Hfq_Ec and Hfq_Pa affected the synthesis of approximately 26 RpoS-independent E. coli gene products. These studies showed that the functional domain of Hfq resides within its N-terminal domain. The observation that a C-terminally truncated Hfq_Ec lacking the last 27 aa [Hfq_Ec(75)] can also functionally replace the full-length E. coli protein lends further support to this notion.

Keywords: global regulator, Hfq, ompA, rpoS

Abbreviations: Hfq_Ec, Hfq protein of Escherichia coli; Hfq_Ec(75), C-terminally truncated Hfq_Ec, lacking the last 27 aa; Hfq_Pa, Hfq homologue of Pseudomonas aeruginosa; UTR, untranslated region

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