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In Vitro S-Glutathionylation of S-Nitrosoglutathione Reductase from Arabidopsis Thaliana and Phenotype Determination of Sensitive to Formaldehyde 1 Knockout Strains of Saccharomyces Cerevisiae

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dc.contributor.advisorElizabeth Vierling
dc.contributor.advisorStephen Eyles
dc.contributor.advisorEric Strieter
dc.contributor.authorTruebridge, Ian
dc.contributor.departmentUniversity of Massachusetts Amherst
dc.contributor.departmentBiochemistry
dc.date2024-03-28T20:13:10.000
dc.date.accessioned2024-04-26T18:23:30Z
dc.date.available2024-04-26T18:23:30Z
dc.date.submittedFebruary
dc.date.submitted2018
dc.description.abstractCells are constantly exposed to different stresses – one being redox stress, which is induced by metal, reactive oxygen species and reactive nitrogen species. S-nitrosoglutathione reductase (GSNOR) helps modulate redox stress by two different mechanisms – either by reducing S-nitrosoglutathione (GSNO) to oxidized glutathione (GSSG) or by oxidizing hydroxymethyl glutathione (HMGSH), a biproduct of glutathione and formaldehyde, to formic acid. GSNO has the potential to posttranslational modify proteins in two different manners, either by S-nitrosation or by S-glutathionylation. Interestingly, GSNOR can be modified by its substrate GSNO, either by S-nitrosation, which has previously been reported, or, as discussed in this thesis, by S-glutathionylation. As S-glutathionylation has been reported to occur through intermediate species, the S-glutathionylation of GSNOR appears to occur though the S-nitrosated intermediate, instead of the most common route of an oxidation pathway. It is hypothesized that the S-glutathionylation, and the overall presence of glutathione, can act as a buffer to regulate the amount of nitrosation that GSNOR experiences, and thus the enzymatic activity. It is has reported that the S-nitrosation occurs on three different non-structural, non-catalytic, solvent-accessible cysteine residues. Experimentation was conducted using Saccharomyces cerevisiae as a model organism to determine how those three cysteine residues of the GSNOR homolog Sensitive to Formaldehyde 1 (SFA1) participate in the indirect detoxification of formaldehyde, through the hydroxymethyl glutathione pathway. It has been determined that cysteine 370 is not as important as previously thought, but the other one or two cysteines (either cysteine 10 or 271) do indeed play a role in the detoxification, but further analysis needs to be conducted.
dc.description.degreeMaster of Science (M.S.)
dc.identifier.doihttps://doi.org/10.7275/11188699
dc.identifier.orcidN/A
dc.identifier.urihttps://hdl.handle.net/20.500.14394/33652
dc.relation.urlhttps://scholarworks.umass.edu/cgi/viewcontent.cgi?article=1636&context=masters_theses_2&unstamped=1
dc.source.statuspublished
dc.subjectS-glutathionylation
dc.subjectS-nitrosoglutathione reductase
dc.subjectArabidopsis thaliana
dc.subjectBiochemistry
dc.titleIn Vitro S-Glutathionylation of S-Nitrosoglutathione Reductase from Arabidopsis Thaliana and Phenotype Determination of Sensitive to Formaldehyde 1 Knockout Strains of Saccharomyces Cerevisiae
dc.typeopenaccess
dc.typearticle
dc.typethesis
digcom.contributor.authorisAuthorOfPublication|email:itruebri@umass.edu|institution:University of Massachusetts Amherst|Truebridge, Ian
digcom.identifiermasters_theses_2/618
digcom.identifier.contextkey11188699
digcom.identifier.submissionpathmasters_theses_2/618
dspace.entity.typePublication
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