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Article: Photo-lysine captures proteins that bind lysine post-translational modifications

TitlePhoto-lysine captures proteins that bind lysine post-translational modifications
Authors
Yang, TLi, XBao, XFung, EYMLi, X
Issue Date2016
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/naturechemicalbiology
Citation
Nature Chemical Biology, 2016, v. 12 n. 2, p. 70-72 How to Cite?
DOI: http://dx.doi.org/10.1038/nchembio.1990
AbstractPost-translational modifications (PTMs) have key roles in regulating protein-protein interactions in living cells. However, it remains a challenge to identify these PTM-mediated interactions. Here we develop a new lysine-based photo-reactive amino acid, termed photo-lysine. We demonstrate that photo-lysine, which is readily incorporated into proteins by native mammalian translation machinery, can be used to capture and identify proteins that recognize lysine PTMs, including 'readers' and 'erasers' of histone modifications.
Persistent Identifierhttp://hdl.handle.net/10722/222443
ISSN
1552-4450
2021 Impact Factor: 16.174
2020 SCImago Journal Rankings: 6.412
ISI Accession Number ID
WOS:000369317300006
Grants
Novel Structure and Function of Human Sirtuins

 

DC FieldValueLanguage
dc.contributor.authorYang, T-
dc.contributor.authorLi, X-
dc.contributor.authorBao, X-
dc.contributor.authorFung, EYM-
dc.contributor.authorLi, X-
dc.date.accessioned2016-01-18T07:40:02Z-
dc.date.available2016-01-18T07:40:02Z-
dc.date.issued2016-
dc.identifier.citationNature Chemical Biology, 2016, v. 12 n. 2, p. 70-72-
dc.identifier.issn1552-4450-
dc.identifier.urihttp://hdl.handle.net/10722/222443-
dc.description.abstractPost-translational modifications (PTMs) have key roles in regulating protein-protein interactions in living cells. However, it remains a challenge to identify these PTM-mediated interactions. Here we develop a new lysine-based photo-reactive amino acid, termed photo-lysine. We demonstrate that photo-lysine, which is readily incorporated into proteins by native mammalian translation machinery, can be used to capture and identify proteins that recognize lysine PTMs, including 'readers' and 'erasers' of histone modifications.-
dc.languageeng-
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/naturechemicalbiology-
dc.relation.ispartofNature Chemical Biology-
dc.titlePhoto-lysine captures proteins that bind lysine post-translational modifications-
dc.typeArticle-
dc.identifier.emailFung, EYM: eva.fungym@hku.hk-
dc.identifier.emailLi, X: xiangli@hku.hk-
dc.identifier.authorityFung, EYM=rp01986-
dc.identifier.authorityLi, X=rp01562-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1038/nchembio.1990-
dc.identifier.pmid26689789-
dc.identifier.scopuseid_2-s2.0-84955758487-
dc.identifier.hkuros256644-
dc.identifier.volume12-
dc.identifier.issue2-
dc.identifier.spage70-
dc.identifier.epage72-
dc.identifier.eissn1552-4469-
dc.identifier.isiWOS:000369317300006-
dc.relation.projectNovel Structure and Function of Human Sirtuins-
dc.identifier.issnl1552-4450-

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