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Article: Identification of the YEATS domain of GAS41 as a pH-dependent reader of histone succinylation

TitleIdentification of the YEATS domain of GAS41 as a pH-dependent reader of histone succinylation
Authors
KeywordsSuccinyl-lysine
Reader
GAS41
Issue Date2018
PublisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.org
Citation
Proceedings of the National Academy of Sciences, 2018, v. 115 n. 10, p. 2365-2370 How to Cite?
AbstractLysine succinylation is a newly discovered posttranslational modification with distinctive physical properties. However, to date rarely have studies reported effectors capable of interpreting this modification on histones. Following our previous study of SIRT5 as an eraser of succinyl-lysine (Ksuc), here we identified the GAS41 YEATS domain as a reader of Ksuc on histones. Biochemical studies showed that the GAS41 YEATS domain presents significant binding affinity toward H3K122suc upon a protonated histidine residue. Furthermore, cellular studies showed that GAS41 had prominent interaction with H3K122suc on histones and also demonstrated the coenrichment of GAS41 and H3K122suc on the p21 promoter. To investigate the binding mechanism, we solved the crystal structure of the YEATS domain of Yaf9, the GAS41 homolog, in complex with an H3K122suc peptide that demonstrated the presence of a salt bridge formed when a protonated histidine residue (His39) recognizes the carboxyl terminal of the succinyl group. We also solved the apo structure of GAS41 YEATS domain, in which the conserved His43 residue superimposes well with His39 in the Yaf9 structure. Our findings identified a reader of succinyl-lysine, and the binding mechanism will provide insight into the development of specific regulators targeting GAS41.
Persistent Identifierhttp://hdl.handle.net/10722/260300
ISSN
2023 Impact Factor: 9.4
2023 SCImago Journal Rankings: 3.737
PubMed Central ID
ISI Accession Number ID
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DC FieldValueLanguage
dc.contributor.authorWang, Y-
dc.contributor.authorJin, J-
dc.contributor.authorCHUNG, WH-
dc.contributor.authorFeng, L-
dc.contributor.authorSun, H-
dc.contributor.authorHao, Q-
dc.date.accessioned2018-09-14T08:39:21Z-
dc.date.available2018-09-14T08:39:21Z-
dc.date.issued2018-
dc.identifier.citationProceedings of the National Academy of Sciences, 2018, v. 115 n. 10, p. 2365-2370-
dc.identifier.issn0027-8424-
dc.identifier.urihttp://hdl.handle.net/10722/260300-
dc.description.abstractLysine succinylation is a newly discovered posttranslational modification with distinctive physical properties. However, to date rarely have studies reported effectors capable of interpreting this modification on histones. Following our previous study of SIRT5 as an eraser of succinyl-lysine (Ksuc), here we identified the GAS41 YEATS domain as a reader of Ksuc on histones. Biochemical studies showed that the GAS41 YEATS domain presents significant binding affinity toward H3K122suc upon a protonated histidine residue. Furthermore, cellular studies showed that GAS41 had prominent interaction with H3K122suc on histones and also demonstrated the coenrichment of GAS41 and H3K122suc on the p21 promoter. To investigate the binding mechanism, we solved the crystal structure of the YEATS domain of Yaf9, the GAS41 homolog, in complex with an H3K122suc peptide that demonstrated the presence of a salt bridge formed when a protonated histidine residue (His39) recognizes the carboxyl terminal of the succinyl group. We also solved the apo structure of GAS41 YEATS domain, in which the conserved His43 residue superimposes well with His39 in the Yaf9 structure. Our findings identified a reader of succinyl-lysine, and the binding mechanism will provide insight into the development of specific regulators targeting GAS41.-
dc.languageeng-
dc.publisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.org-
dc.relation.ispartofProceedings of the National Academy of Sciences-
dc.subjectSuccinyl-lysine-
dc.subjectReader-
dc.subjectGAS41-
dc.titleIdentification of the YEATS domain of GAS41 as a pH-dependent reader of histone succinylation-
dc.typeArticle-
dc.identifier.emailJin, J: jinjing@hku.hk-
dc.identifier.emailHao, Q: qhao@hku.hk-
dc.identifier.authorityWang, Y=rp02093-
dc.identifier.authorityHao, Q=rp01332-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1073/pnas.1717664115-
dc.identifier.pmid29463709-
dc.identifier.pmcidPMC5877980-
dc.identifier.scopuseid_2-s2.0-85042917384-
dc.identifier.hkuros290904-
dc.identifier.volume115-
dc.identifier.issue10-
dc.identifier.spage2365-
dc.identifier.epage2370-
dc.identifier.isiWOS:000426671900062-
dc.publisher.placeUnited States-
dc.relation.projectNovel Structure and Function of Human Sirtuins-
dc.identifier.issnl0027-8424-

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