dc.contributor.author | Yin, Yeshi | |
dc.contributor.author | Withers, T. Ryan | |
dc.contributor.author | Wang, Xin | |
dc.contributor.author | Yu, Hongwei D. | |
dc.contributor.author | de Regt, Anna Katherine | |
dc.contributor.author | Baker, Tania | |
dc.contributor.author | Sauer, Robert T. | |
dc.date.accessioned | 2017-01-11T16:14:44Z | |
dc.date.available | 2017-01-11T16:14:44Z | |
dc.date.issued | 2014-07 | |
dc.date.submitted | 2014-06 | |
dc.identifier.issn | 0950-382X | |
dc.identifier.issn | 1365-2958 | |
dc.identifier.uri | http://hdl.handle.net/1721.1/106340 | |
dc.description.abstract | 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 MucA in 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. | en_US |
dc.description.sponsorship | United States. National Aeronautics and Space Administration. West Virginia Space Grant Consortium | en_US |
dc.description.sponsorship | Canadian Cystic Fibrosis Foundation (Grant CFF-YU11G0) | en_US |
dc.description.sponsorship | National Institutes of Health (U.S.) (Grant AI-16892) | en_US |
dc.language.iso | en_US | |
dc.publisher | Wiley Blackwell | en_US |
dc.relation.isversionof | http://dx.doi.org/10.1111/mmi.12665 | en_US |
dc.rights | Creative Commons Attribution-Noncommercial-Share Alike | en_US |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | en_US |
dc.source | PMC | en_US |
dc.title | Overexpression of CupB5 activates alginate overproduction in Pseudomonas aeruginosa by a novel AlgW-dependent mechanism | en_US |
dc.type | Article | en_US |
dc.identifier.citation | de Regt, Anna K. et al. “Overexpression of CupB5 Activates Alginate Overproduction in P Seudomonas Aeruginosa by a Novel AlgW-Dependent Mechanism: CupB5 Activates Alginate Production through AlgW.” Molecular Microbiology 93.3 (2014): 415–425. | en_US |
dc.contributor.department | Massachusetts Institute of Technology. Department of Biology | en_US |
dc.contributor.mitauthor | de Regt, Anna Katherine | |
dc.contributor.mitauthor | Baker, Tania | |
dc.contributor.mitauthor | Sauer, Robert T. | |
dc.relation.journal | Molecular Microbiology | en_US |
dc.eprint.version | Author's final manuscript | en_US |
dc.type.uri | http://purl.org/eprint/type/JournalArticle | en_US |
eprint.status | http://purl.org/eprint/status/PeerReviewed | en_US |
dspace.orderedauthors | de Regt, Anna K.; Yin, Yeshi; Withers, T. Ryan; Wang, Xin; Baker, Tania A.; Sauer, Robert T.; Yu, Hongwei D. | en_US |
dspace.embargo.terms | N | en_US |
dc.identifier.orcid | https://orcid.org/0000-0002-1719-5399 | |
dspace.mitauthor.error | true | |
mit.license | OPEN_ACCESS_POLICY | en_US |