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Article: Use of Serine/Threonine Ligation for the Total Chemical Synthesis of HMGA1a Protein with Site‐Specific Lysine Acetylations

TitleUse of Serine/Threonine Ligation for the Total Chemical Synthesis of HMGA1a Protein with Site‐Specific Lysine Acetylations
Authors
Liu, HLiu, HLi, X
KeywordsAcetylation
HMG proteins
Kinase assays
Post-translational modifications
Ser/Thr ligation
Issue Date2019
PublisherWiley - V C H Verlag GmbH & Co. KGaA. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1002/%28ISSN%292192-6506
Citation
ChemPlusChem, 2019, v. 84 n. 7, p. 779-785 How to Cite?
DOI: http://dx.doi.org/10.1002/cplu.201900130
AbstractHigh‐mobility‐group (HMG) proteins are a class of abundant non‐histone nuclear proteins, among which HMGA1a is well‐known for its association with transcription regulation as well as tumor formation and disease development. To study the functions of post‐translational modifications, homogeneous HMGA1a protein with site‐specific lysine acetylations (64/66/70/73) has been chemically synthesized. The full‐length HMGA1a protein was assembled through two Ser/Thr ligations of three peptide fragments at Gly37‐Thr37 and Thr75‐Thr76 sites, respectively. Further in vitro studies with chemically synthesized proteins suggested that these acetylations did not significantly affect the CK2‐catalyzed phosphorylation on the HMGA1a acidic tail.
Persistent Identifierhttp://hdl.handle.net/10722/272141
ISSN
2192-6506
2023 Impact Factor: 3.0
2023 SCImago Journal Rankings: 0.778
ISI Accession Number ID
WOS:000477962500002

 

DC FieldValueLanguage
dc.contributor.authorLiu, H-
dc.contributor.authorLiu, H-
dc.contributor.authorLi, X-
dc.date.accessioned2019-07-20T10:36:27Z-
dc.date.available2019-07-20T10:36:27Z-
dc.date.issued2019-
dc.identifier.citationChemPlusChem, 2019, v. 84 n. 7, p. 779-785-
dc.identifier.issn2192-6506-
dc.identifier.urihttp://hdl.handle.net/10722/272141-
dc.description.abstractHigh‐mobility‐group (HMG) proteins are a class of abundant non‐histone nuclear proteins, among which HMGA1a is well‐known for its association with transcription regulation as well as tumor formation and disease development. To study the functions of post‐translational modifications, homogeneous HMGA1a protein with site‐specific lysine acetylations (64/66/70/73) has been chemically synthesized. The full‐length HMGA1a protein was assembled through two Ser/Thr ligations of three peptide fragments at Gly37‐Thr37 and Thr75‐Thr76 sites, respectively. Further in vitro studies with chemically synthesized proteins suggested that these acetylations did not significantly affect the CK2‐catalyzed phosphorylation on the HMGA1a acidic tail.-
dc.languageeng-
dc.publisherWiley - V C H Verlag GmbH & Co. KGaA. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1002/%28ISSN%292192-6506-
dc.relation.ispartofChemPlusChem-
dc.subjectAcetylation-
dc.subjectHMG proteins-
dc.subjectKinase assays-
dc.subjectPost-translational modifications-
dc.subjectSer/Thr ligation-
dc.titleUse of Serine/Threonine Ligation for the Total Chemical Synthesis of HMGA1a Protein with Site‐Specific Lysine Acetylations-
dc.typeArticle-
dc.identifier.emailLi, X: xuechenl@hku.hk-
dc.identifier.authorityLi, X=rp00742-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/cplu.201900130-
dc.identifier.pmid31943990-
dc.identifier.scopuseid_2-s2.0-85065195494-
dc.identifier.hkuros299165-
dc.identifier.volume84-
dc.identifier.issue7-
dc.identifier.spage779-
dc.identifier.epage785-
dc.identifier.isiWOS:000477962500002-
dc.publisher.placeGermany-
dc.identifier.issnl2192-6506-

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