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dc.contributor.authorShu, Xin
dc.contributor.authorAsghar, Sana
dc.contributor.authorYang, Fan
dc.contributor.authorLi, Shang-Tong
dc.contributor.authorWu, Haifan
dc.contributor.authorYang, Bing
dc.date.accessioned2022-04-08T21:48:10Z
dc.date.available2022-04-08T21:48:10Z
dc.date.issued2022-02-18
dc.identifier.citationShu X, Asghar S, Yang F, Li S-T, Wu H and Yang B (2022) Uncover New Reactivity of Genetically Encoded Alkyl Bromide Non-Canonical Amino Acids. Front. Chem. 10:815991. doi: 10.3389/fchem.2022.815991en_US
dc.identifier.issn22962646
dc.identifier.urihttps://doi.org/10.3389/fchem.2022.815991
dc.identifier.urihttps://soar.wichita.edu/handle/10057/23027
dc.descriptionThis is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.en_US
dc.description.abstractGenetically encoded non-canonical amino acids (ncAAs) with electrophilic moieties are excellent tools to investigate protein-protein interactions (PPIs) both in vitro and in vivo. These ncAAs, including a series of alkyl bromide-based ncAAs, mainly target cysteine residues to form protein-protein cross-links. Although some reactivities towards lysine and tyrosine residues have been reported, a comprehensive understanding of their reactivity towards a broad range of nucleophilic amino acids is lacking. Here we used a recently developed OpenUaa search engine to perform an in-depth analysis of mass spec data generated for Thioredoxin and its direct binding proteins cross-linked with an alkyl bromide-based ncAA, BprY. The analysis showed that, besides cysteine residues, BprY also targeted a broad range of nucleophilic amino acids. We validated this broad reactivity of BprY with Affibody/Z protein complex. We then successfully applied BprY to map a binding interface between SUMO2 and SUMO-interacting motifs (SIMs). BprY was further applied to probe SUMO2 interaction partners. We identified 264 SUMO2 binders, including several validated SUMO2 binders and many new binders. Our data demonstrated that BprY can be effectively used to probe protein-protein interaction interfaces even without cysteine residues, which will greatly expand the power of BprY in studying PPIs.en_US
dc.description.sponsorshipThis work was supported by the Chinese National Natural Science Funds (91953103 and 22074132 to BY), the special COVID-19 program of the Sino-German Center for Research Promotion (C-0023 to BY), the outstanding youth fund of Zhejiang Province (LR20B050001 to BY), Open Project Program of the State Key Laboratory of Proteomics (SKLPO201806 to BY), and startup fund provided by Wichita State University to H.W.en_US
dc.language.isoen_USen_US
dc.publisherFrontiers Media S.A.en_US
dc.relation.ispartofseriesFrontiers in Chemistry;2022
dc.subjectProtein-protein interactionsen_US
dc.subjectGenetic code expansionen_US
dc.subjectNon-canonical amino aciden_US
dc.subjectChemical cross-linkingen_US
dc.subjectSUMO interactomeen_US
dc.titleUncover new reactivity of genetically encoded alkyl bromide non-canonical amino acidsen_US
dc.typeArticleen_US
dc.rights.holder2022 Shu, Asghar, Yang, Li, Wu and Yang.en_US


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