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dc.contributor.authorRajeev, L.
dc.contributor.authorLuning, E. G.
dc.contributor.authorAltenburg, Sara
dc.contributor.authorZane, Grant M.
dc.contributor.authorBaidoo, Edward E. K.
dc.contributor.authorCatena, M.
dc.contributor.authorKeasling, J. D.
dc.contributor.authorWall, Judy D.
dc.contributor.authorFields, Matthew W.
dc.contributor.authorMukhopadhyay, A.
dc.date.accessioned2016-12-05T16:38:14Z
dc.date.available2016-12-05T16:38:14Z
dc.date.issued2014-07
dc.identifier.citationRajeev L, Luning EG, Altenburg S, Zane GM, Baidoo EE, Catena M, Keasling JD, Wall JD, Fields MW, Mukhopadhyay A, "Identification of a cyclic-di-GMP-modulating response regulator that impacts biofilm formation in a model sulfate reducing bacterium," Front Microbiol. July 2014 5:382.en_US
dc.identifier.issn1664-302X
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/12299
dc.description.abstractWe surveyed the eight putative cyclic-di-GMP-modulating response regulators (RRs) in Desulfovibrio vulgaris Hildenborough that are predicted to function via two-component signaling. Using purified proteins, we examined cyclic-di-GMP (c-di-GMP) production or turnover in vitro of all eight proteins. The two RRs containing only GGDEF domains (DVU2067, DVU0636) demonstrated c-di-GMP production activity in vitro. Of the remaining proteins, three RRs with HD-GYP domains (DVU0722, DVUA0086, and DVU2933) were confirmed to be Mn(2+)-dependent phosphodiesterases (PDEs) in vitro and converted c-di-GMP to its linear form, pGpG. DVU0408, containing both c-di-GMP production (GGDEF) and degradation domains (EAL), showed c-di-GMP turnover activity in vitro also with production of pGpG. No c-di-GMP related activity could be assigned to the RR DVU0330, containing a metal-dependent phosphohydrolase HD-OD domain, or to the HD-GYP domain RR, DVU1181. Studies included examining the impact of overexpressed cyclic-di-GMP-modulating RRs in the heterologous host E. coli and led to the identification of one RR, DVU0636, with increased cellulose production. Evaluation of a transposon mutant in DVU0636 indicated that the strain was impaired in biofilm formation and demonstrated an altered carbohydrate:protein ratio relative to the D. vulgaris wild type biofilms. However, grown in liquid lactate/sulfate medium, the DVU0636 transposon mutant showed no growth impairment relative to the wild-type strain. Among the eight candidates, only the transposon disruption mutant in the DVU2067 RR presented a growth defect in liquid culture. Our results indicate that, of the two diguanylate cyclases (DGCs) that function as part of two-component signaling, DVU0636 plays an important role in biofilm formation while the function of DVU2067 has pertinence in planktonic growth.en_US
dc.rightsCC BY 4.0en_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/legalcodeen_US
dc.titleIdentification of a cyclic-di-GMP-modulating response regulator that impacts biofilm formation in a model sulfate reducing bacteriumen_US
dc.typeArticleen_US
mus.citation.extentfirstpage382en_US
mus.citation.journaltitleFrontiers in Microbiologyen_US
mus.citation.volume5en_US
mus.identifier.categoryChemical & Material Sciencesen_US
mus.identifier.categoryEngineering & Computer Scienceen_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.3389/fmicb.2014.00382en_US
mus.relation.collegeCollege of Agricultureen_US
mus.relation.collegeCollege of Engineeringen_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentCell Biology & Neuroscience.en_US
mus.relation.departmentCenter for Biofilm Engineering.en_US
mus.relation.departmentChemical & Biological Engineering.en_US
mus.relation.departmentChemistry & Biochemistry.en_US
mus.relation.departmentMicrobiology & Immunology.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.relation.researchgroupCenter for Biofilm Engineering.en_US
mus.data.thumbpage2en_US
mus.contributor.orcidFields, Matthew W.|0000-0001-9053-1849en_US


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