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dc.contributor.authorKamal, Shady Mansour
dc.contributor.authorRybtke, Morten Levin
dc.contributor.authorNIMTZ, MANFRED
dc.contributor.authorSperlein, Stefanie
dc.contributor.authorGiske, Christian
dc.contributor.authorTrček, Janja
dc.contributor.authorDeschamps, Julien
dc.contributor.authorBriandet, Romain
dc.contributor.authorDini, Luciana
dc.contributor.authorJänsch, Lothar
dc.contributor.authorTolker-Nielsen, Tim
dc.contributor.authorLee, Changhan
dc.contributor.authorRömling, Ute
dc.date.accessioned2019-08-20T14:34:51Z
dc.date.available2019-08-20T14:34:51Z
dc.date.issued2019-01-01
dc.identifier.issn1664-302X
dc.identifier.pmid31338071
dc.identifier.doi10.3389/fmicb.2019.01372
dc.identifier.urihttp://hdl.handle.net/10033/621912
dc.description.abstractPseudomonas aeruginosa is an environmental bacterium and a nosocomial pathogen with clone C one of the most prevalent clonal groups. The P. aeruginosa clone C specific genomic island PACGI-1 harbors a xenolog of ftsH encoding a functionally diverse membrane-spanning ATP-dependent metalloprotease on the core genome. In the aquatic isolate P. aeruginosa SG17M, the core genome copy ftsH1 significantly affects growth and dominantly mediates a broad range of phenotypes, such as secretion of secondary metabolites, swimming and twitching motility and resistance to aminoglycosides, while the PACGI-1 xenolog ftsH2 backs up the phenotypes in the ftsH1 mutant background. The two proteins, with conserved motifs for disaggregase and protease activity present in FtsH1 and FtsH2, have the ability to form homo- and hetero-oligomers with ftsH2 distinctively expressed in the late stationary phase of growth. However, mainly FtsH1 degrades a major substrate, the heat shock transcription factor RpoH. Pull-down experiments with substrate trap-variants inactive in proteolytic activity indicate both FtsH1 and FtsH2 to interact with the inhibitory protein HflC, while the phenazine biosynthesis protein PhzC was identified as a substrate of FtsH1. In summary, as an exception in P. aeruginosa, clone C harbors two copies of the ftsH metallo-protease, which cumulatively are required for the expression of a diversity of phenotypes.en_US
dc.language.isoenen_US
dc.publisherFrontiersen_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subjectFtsH proteaseen_US
dc.subjectPseudomonas aeruginosaen_US
dc.subjectautolysisen_US
dc.subjectclone C strainsen_US
dc.subjectheat shock factor RpoHen_US
dc.subjectphenazineen_US
dc.subjectsecondary metaboliteen_US
dc.subjectvirulenceen_US
dc.titleTwo FtsH Proteases Contribute to Fitness and Adaptation of Clone C Strains.en_US
dc.typeArticleen_US
dc.contributor.departmentHZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.en_US
dc.identifier.journalFrontiers in Microbiologyen_US
refterms.dateFOA2019-08-20T14:34:51Z
dc.source.journaltitleFrontiers in microbiology


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