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dc.contributor.authorChen, Wen
dc.contributor.authorLi, Lingyun
dc.contributor.authorDu, Zhenming
dc.contributor.authorLiu, Jiajing
dc.contributor.authorReitter, Julie N.
dc.contributor.authorMills, Kenneth V.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorWang, Chunyu
dc.date2012
dc.date.accessioned2022-06-23T04:11:25Z
dc.date.available2022-06-23T04:11:25Z
dc.date.issued2012-02-08
dc.identifier.citationIntramolecular Disulfide Bond between Catalytic Cysteines in an Intein Precursor, W. Chen, L. Li, Z. Du, J. Liu, J. Reitter, K. Mills, R. J. Linhardt, C. Wang, Journal of the American Chemical Society, 134, 2500-2503, 2012.
dc.identifier.issn15205126
dc.identifier.issn27863
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5268
dc.identifier.urihttps://doi.org/10.1021/ja211010g
dc.descriptionJournal of the American Chemical Society, 134, 2500-2503
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractProtein splicing is a self-catalyzed and spontaneous post-translational process in which inteins excise themselves out of precursor proteins while the exteins are ligated together. We report the first discovery of an intramolecular disulfide bond between the two active-site cysteines, Cys1 and Cys+1, in an intein precursor composed of the hyperthermophilic Pyrococcus abyssi PolII intein and extein. The existence of this intramolecular disulfide bond is demonstrated by the effect of reducing agents on the precursor, mutagenesis, and liquid chromatography-mass spectrometry (LC-MS) with tandem MS (MS/MS) of the tryptic peptide containing the intramolecular disulfide bond. The disulfide bond inhibits protein splicing, and splicing can be induced by reducing agents such as tris(2-carboxyethyl)phosphine (TCEP). The stability of the intramolecular disulfide bond is enhanced by electrostatic interactions between the N- and C-exteins but is reduced by elevated temperature. The presence of this intramolecular disulfide bond may contribute to the redox control of splicing activity in hypoxia and at low temperature and point to the intriguing possibility that inteins may act as switches to control extein function.
dc.description.sponsorshipNational Science Foundation
dc.languageen_US
dc.language.isoENG
dc.publisherAmerican Chemical Society (ACS)
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofJournal of the American Chemical Society
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleIntramolecular Disulfide Bond between Catalytic Cysteines in an Intein Precursor
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1021/ja211010g
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages2500-2503
rpi.description.volume134


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