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Use of Serine/Threonine Ligation for the Total Chemical Synthesis of HMGA1a Protein with Site‐Specific Lysine Acetylations
Author(s) -
Liu Heng,
Liu Han,
Li Xuechen
Publication year - 2019
Publication title -
chempluschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.801
H-Index - 61
ISSN - 2192-6506
DOI - 10.1002/cplu.201900130
Subject(s) - acetylation , threonine , lysine , chemistry , serine , phosphorylation , biochemistry , histone , peptide , amino acid , dna , gene
High‐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.