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dc.contributor.authorNicastri, Michael C.
dc.contributor.authorXega, Kristina
dc.contributor.authorLi, Lingyun
dc.contributor.authorXie, Jian
dc.contributor.authorWang, Chunyu
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorReitter, Julie N.
dc.contributor.authorMills, Kenneth V.
dc.date2013
dc.date.accessioned2022-06-23T04:17:30Z
dc.date.available2022-06-23T04:17:30Z
dc.date.issued2013-08-27
dc.identifier.citationInternal disulfide bond acts as a switch for intein activity, M.C. Nicastri, K. Xega, L. Li, J.Xie, C. Wang, R.J. Linhardt, J.N. Reitter, K. V. Mills, Biochemistry, 52, 5920–5927, 2013.
dc.identifier.issn15204995
dc.identifier.issn62960
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5314
dc.identifier.urihttps://doi.org/10.1021/bi400736c
dc.descriptionBiochemistry, 52, 5920–5927
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.abstractInteins are intervening polypeptides that catalyze their own removal from flanking exteins, concomitant to the ligation of the exteins. The intein that interrupts the DP2 (large) subunit of DNA polymerase II from Methanoculleus marisnigri (Mma) can promote protein splicing. However, protein splicing can be prevented or reduced by overexpression under nonreducing conditions because of the formation of a disulfide bond between two internal intein Cys residues. This redox sensitivity leads to differential activity in different strains of E. coli as well as in different cell compartments. The redox-dependent control of in vivo protein splicing in an intein derived from an anaerobe that can occupy multiple environments hints at a possible physiological role for protein splicing.
dc.description.sponsorshipNational Institute of General Medical Sciences
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.ispartofBiochemistry
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleInternal disulfide bond acts as a switch for intein activity
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1021/bi400736c
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.pages5920-5927
rpi.description.volume52


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