Show simple item record

dc.contributor.authorChand, Nikhilesh
dc.contributor.authorClatworthy, Anne
dc.contributor.authorHung, Deborah
dc.date.accessioned2019-10-13T16:02:50Z
dc.date.issued2012
dc.identifier.citationChand, Nikhilesh S., Anne E. Clatworthy, and Deborah T. Hung. 2012. “The Two-Component Sensor KinB Acts as a Phosphatase To Regulate Pseudomonas Aeruginosa Virulence.” Journal of Bacteriology 194 (23): 6537–47. doi:10.1128/JB.01168-12.
dc.identifier.issn0021-9193
dc.identifier.issn1067-8832
dc.identifier.issn1098-5530
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:41542758*
dc.description.abstractPseudomonas aeruginosa is an opportunistic pathogen that is capable of causing both acute and chronic infections. P. aeruginosa virulence is subject to sophisticated regulatory control by two-component systems that enable it to sense and respond to environmental stimuli. We recently reported that the two-component sensor KinB regulates virulence in acute P. aeruginosa infection. Furthermore, it regulates acute-virulence-associated phenotypes such as pyocyanin production, elastase production, and motility in a manner independent of its kinase activity. Here we show that KinB regulates virulence through the global sigma factor AlgU, which plays a key role in repressing P. aeruginosa acute-virulence factors, and through its cognate response regulator AlgB. However, we show that rather than phosphorylating AlgB, KinB's primary role in the regulation of virulence is to act as a phosphatase to dephosphorylate AlgB and alleviate phosphorylated AlgB's repression of acute virulence.
dc.language.isoen_US
dc.publisherAmerican Society for Microbiology
dash.licenseLAA
dc.titleThe Two-Component Sensor KinB Acts as a Phosphatase to Regulate Pseudomonas aeruginosa Virulence
dc.typeJournal Article
dc.description.versionVersion of Record
dc.relation.journalJournal of Bacteriology
dash.depositing.authorHung, Deborah Tan::45968263d9ae67f8c1970987265073e7::600
dc.date.available2019-10-13T16:02:50Z
dash.workflow.comments1Science Serial ID 51164
dc.identifier.doi10.1128/JB.01168-12
dash.source.volume194;23
dash.source.page6537


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record