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Overexpression of CupB5 activates alginate overproduction in Pseudomonas aeruginosa by a novel AlgW-dependent mechanism

文献类型： 外文期刊

作者： de Regt, Anna K. 1 ; Yin, Yeshi 2 ; Withers, T. Ryan 2 ; Wang, Xin 4 ; Baker, Tania A. 1 ; Sauer, Robert T. 1 ; Yu, Ho 1 ;

作者机构： 1.MIT, Dept Biol, Cambridge, MA 02139 USA

2.Marshall Univ, Dept Biochem & Microbiol, Joan C Edwards Sch Med, Huntington, WV 25755 USA

3.Marshall Univ, Dept Pediat, Joan C Edwards Sch Med, Huntington, WV 25755 USA

4.Zhejiang Acad Agr Sci, Inst Plant Protect & Microbiol, Hangzhou 310021, Zhejiang, Peoples R China

5.Progenesis Technol LLC, Huntington, WV 25701 USA

期刊名称：MOLECULAR MICROBIOLOGY （ 影响因子：3.501； 五年影响因子：3.996 ）

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收录情况： SCI

摘要： In Pseudomonas aeruginosa, alginate overproduction, also known as mucoidy, is negatively regulated by the transmembrane protein MucA, which sequesters the alternative sigma factor AlgU. MucA is degraded via a proteolysis pathway that frees AlgU from sequestration, activating alginate biosynthesis. Initiation of this pathway normally requires two signals: peptide sequences in unassembled outer-membrane proteins (OMPs) activate the AlgW protease, and unassembled lipopolysaccharides bind periplasmic MucB, releasing MucA and facilitating its proteolysis by activated AlgW. To search for novel alginate regulators, we screened a transposon library in the non-mucoid reference strain PAO1, and identified a mutant that confers mucoidy through overexpression of a protein encoded by the chaperone-usher pathway gene cupB5. CupB5-dependent mucoidy occurs through the AlgU pathway and can be reversed by overexpression of MucA or MucB. In the presence of activating OMP peptides, peptides corresponding to a region of CupB5 needed for mucoidy further stimulated AlgW cleavage of MucAin vitro. Moreover, the CupB5 peptide allowed OMP-activated AlgW cleavage of MucA in the presence of the MucB inhibitor. These results support a novel mechanism for conversion to mucoidy in which the proteolytic activity of AlgW and its ability to compete with MucB for MucA is mediated by independent peptide signals.

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