Expression and purification of untagged GlnK proteins from actinobacteria

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dc.contributor.authorGerhardt, Edileusa C.M.
dc.contributor.authorMoure, Vivian R.
dc.contributor.authorSouza, Andrey W.
dc.contributor.authorPedrosa, Fabio O.
dc.contributor.authorSouza, Emanuel M.
dc.contributor.authorDiacovich, Lautaro
dc.contributor.authorGramajo, Hugo
dc.contributor.authorHuergo, Luciano F.
dc.date.accessioned2017-11-24T13:22:17Z
dc.date.available2017-11-24T13:22:17Z
dc.date.issued2017-06-27
dc.description.abstractThe PII protein family constitutes one of the most conserved and well distributed family of signal transduction proteins in nature. These proteins play key roles in nitrogen and carbon metabolism. PII function has been well documented in Gram-negative bacteria. However, there are very few reports describing the in vitro properties and function of PII derived from Gram-positive bacteria. Here we present the heterologous expression and efficient purification protocols for untagged PII from three Actinobacteria of medical and biotechnological interest namely: Mycobacterium tuberculosis, Rhodococcus jostii and Streptomyces coelicolor. Circular dichroism and gel filtration analysis supported that the purified proteins are correctly folded. The purification protocol described here will facilitate biochemical studies and help to uncover the biochemical functions of PII proteins in Actinobacteria.en
dc.identifier.issn1611-2156
dc.identifier.urihttp://hdl.handle.net/2003/36199
dc.identifier.urihttp://dx.doi.org/10.17877/DE290R-18213
dc.language.isoen
dc.relation.ispartofseriesEXCLI Journal;Vol. 16 2017
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectPIIen
dc.subjectGlnKen
dc.subjectCD analysisen
dc.subjectactinobacteriaen
dc.subject.ddc610
dc.titleExpression and purification of untagged GlnK proteins from actinobacteriaen
dc.typeText
dc.type.publicationtypearticle
dcterms.accessRightsopen access
eldorado.dnb.zdberstkatid2132560-1
eldorado.secondarypublicationtrue

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