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dc.contributor.authorDye, Keane J.en
dc.contributor.authorYang, Zhaominen
dc.date.accessioned2021-01-13T16:01:18Zen
dc.date.available2021-01-13T16:01:18Zen
dc.date.issued2020-01-10en
dc.identifier.issn0264-6021en
dc.identifier.urihttp://hdl.handle.net/10919/101875en
dc.description.abstractPilB is the assembly ATPase for the bacterial type IV pilus (T4P), and as a consequence, it is essential for T4P-mediated bacterial motility. In some cases, PilB has been demonstrated to regulate the production of exopolysaccharide (EPS) during bacterial biofilm development independently of or in addition to its function in pilus assembly. While the ATPase activity of PilB resides at its C-terminal region, the N terminus of a subset of PilBs forms a novel cyclic-di-GMP (cdG)-binding domain. This multi-domain structure suggests that PilB binds cdG and adenine nucleotides through separate domains which may influence the functionality of PilB in both motility and biofilm development. Here, Chloracidobacterium thermophilum PilB is used to investigate ligand binding by its separate domains and by the full-length protein. Our results confirm the specificity of these individual domains for their respective ligands and demonstrate communications between these domains in the full-length protein. It is clear that when the N- and the C-terminal domains of PilB bind to cdG and ADP, respectively, they mutually influence each other in conformation and in their binding to ligands. We propose that the interactions between these domains in response to their ligands play critical roles in modulating or controlling the functions of PilB as a regulator of EPS production and as the T4P assembly ATPase.en
dc.description.sponsorshipNational Science FoundationNational Science Foundation (NSF) [MCB-1417726, MCB-1919455]en
dc.format.mimetypeapplication/pdfen
dc.language.isoenen
dc.rightsCreative Commons Attribution-NonCommercial-NoDerivs 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/en
dc.titleCyclic-di-GMP and ADP bind to separate domains of PilB as mutual allosteric effectorsen
dc.typeArticle - Refereeden
dc.contributor.departmentBiological Sciencesen
dc.description.notesThis work was supported by National Science Foundation grants MCB-1417726 and MCB-1919455 to Z.Y.en
dc.title.serialBiochemical Journalen
dc.identifier.doihttps://doi.org/10.1042/BCJ20190809en
dc.identifier.volume477en
dc.identifier.issue1en
dc.type.dcmitypeTexten
dc.type.dcmitypeStillImageen
dc.identifier.pmid31868878en
dc.identifier.eissn1470-8728en


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Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International
License: Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International