Detection of glucose-induced conformational change in hexokinase II using fluorescence complementation assay

Cited 4 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorEun-Ju Jeong-
dc.contributor.authorKyoungsook Park-
dc.contributor.authorHyou-Arm Joung-
dc.contributor.authorChang-Soo Lee-
dc.contributor.authorD W Seol-
dc.contributor.authorBong Hyun Chung-
dc.contributor.authorMoonil Kim-
dc.date.accessioned2017-04-19T09:06:50Z-
dc.date.available2017-04-19T09:06:50Z-
dc.date.issued2007-
dc.identifier.issn0141-5492-
dc.identifier.uri10.1007/s10529-007-9313-xko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/7858-
dc.description.abstractConformational changes in hexokinase are induced by its binding to glucose, thus providing an excellent example of an 'induced fit' model. To observe glucose-induced fluorescence restoration in hexokinase II using split-enhanced, green fluorescent protein (EGFP) in a process involving the reconstitution of split EGFP, E. coli cells expressing the chimeric NEGFP:HXK:CEGFP recombinant protein were treated with glucose and visualized via fluorescence read-outs. The reconstituted EGFP generated a strong fluorescence upon glucose stimulation of the bacteria. Moreover, the fluorescence intensity became stronger with increasing glucose up to 10 mM, with a maximum being observed after 60 min in a time- and concentration-dependent manner. Conformational changes associated with glucose-induced fit in human hexokinase II can thus be monitored successfully in vivo via fluorescence reconstitution assays, coupled with a quick and easy fluorescent read-out protocol.-
dc.publisherSpringer-
dc.titleDetection of glucose-induced conformational change in hexokinase II using fluorescence complementation assay-
dc.title.alternativeDetection of glucose-induced conformational change in hexokinase II using fluorescence complementation assay-
dc.typeArticle-
dc.citation.titleBiotechnology Letters-
dc.citation.number5-
dc.citation.endPage802-
dc.citation.startPage797-
dc.citation.volume29-
dc.contributor.affiliatedAuthorEun-Ju Jeong-
dc.contributor.affiliatedAuthorKyoungsook Park-
dc.contributor.affiliatedAuthorChang-Soo Lee-
dc.contributor.affiliatedAuthorBong Hyun Chung-
dc.contributor.affiliatedAuthorMoonil Kim-
dc.contributor.alternativeName정은주-
dc.contributor.alternativeName박경숙-
dc.contributor.alternativeName정효암-
dc.contributor.alternativeName이창수-
dc.contributor.alternativeName설대우-
dc.contributor.alternativeName정봉현-
dc.contributor.alternativeName김문일-
dc.identifier.bibliographicCitationBiotechnology Letters, vol. 29, no. 5, pp. 797-802-
dc.identifier.doi10.1007/s10529-007-9313-x-
dc.subject.keywordConformational change-
dc.subject.keywordFluorescence complementation assay-
dc.subject.keywordGlucose-induced fit-
dc.subject.keywordHexokinase II-
dc.subject.keywordSplit EGFP-
dc.subject.localconformational change-
dc.subject.localConformational change-
dc.subject.localFluorescence complementation assay-
dc.subject.localGlucose-induced fit-
dc.subject.localHexokinase II-
dc.subject.localSplit EGFP-
dc.description.journalClassY-
Appears in Collections:
Division of Research on National Challenges > Bionanotechnology Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.