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dc.contributor.authorPatterson, Angela
dc.contributor.authorWhite, Aidan
dc.contributor.authorWaymire, Elizabeth
dc.contributor.authorFleck, Sophie
dc.contributor.authorGolden, Sarah
dc.contributor.authorWilkinson, Royce A.
dc.contributor.authorWiedenheft, Blake
dc.contributor.authorBothner, Brian
dc.date.accessioned2023-01-25T19:20:01Z
dc.date.available2023-01-25T19:20:01Z
dc.date.issued2022-10
dc.identifier.citationAngela Patterson, Aidan White, Elizabeth Waymire, Sophie Fleck, Sarah Golden, Royce A Wilkinson, Blake Wiedenheft, Brian Bothner, Anti-CRISPR proteins function through thermodynamic tuning and allosteric regulation of CRISPR RNA-guided surveillance complex, Nucleic Acids Research, Volume 50, Issue 19, 28 October 2022, Pages 11243–11254, https://doi.org/10.1093/nar/gkac841en_US
dc.identifier.issn0305-1048
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/17631
dc.description.abstractCRISPR RNA-guided detection and degradation of foreign DNA is a dynamic process. Viruses can interfere with this cellular defense by expressing small proteins called anti-CRISPRs. While structural models of anti-CRISPRs bound to their target complex provide static snapshots that inform mechanism, the dynamics and thermodynamics of these interactions are often overlooked. Here, we use hydrogen deuterium exchange-mass spectrometry (HDX-MS) and differential scanning fluorimetry (DSF) experiments to determine how anti-CRISPR binding impacts the conformational landscape of the type IF CRISPR RNA guided surveillance complex (Csy) upon binding of two different anti-CRISPR proteins (AcrIF9 and AcrIF2). The results demonstrate that AcrIF2 binding relies on enthalpic stabilization, whereas AcrIF9 uses an entropy driven reaction to bind the CRISPR RNA-guided surveillance complex. Collectively, this work reveals the thermodynamic basis and mechanistic versatility of anti-CRISPR-mediated immune suppression. More broadly, this work presents a striking example of how allosteric effectors are employed to regulate nucleoprotein complexes.en_US
dc.language.isoen_USen_US
dc.publisherOxford University Pressen_US
dc.rightscc-byen_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en_US
dc.subjectanti-crispren_US
dc.subjectanti-crispr proteinsen_US
dc.subjectthermodynamic tuningen_US
dc.subjectallosteric regulationen_US
dc.subjectCRISPR RNAen_US
dc.titleAnti-CRISPR proteins function through thermodynamic tuning and allosteric regulation of CRISPR RNA-guided surveillance complexen_US
dc.typeArticleen_US
mus.citation.extentfirstpage1en_US
mus.citation.extentlastpage12en_US
mus.citation.issue19en_US
mus.citation.journaltitleNucleic Acids Researchen_US
mus.citation.volume50en_US
mus.identifier.doi10.1093/nar/gkac841en_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentChemistry & Biochemistry.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.data.thumbpage5en_US


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