Protein lysine de-2-hydroxyisobutyrylation by CobB in prokaryotes.
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ABSTRACT:
SUBMITTER: Dong H
PROVIDER: S-EPMC6636992 | biostudies-literature | 2019 Jul
REPOSITORIES: biostudies-literature
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Protein lysine de-2-hydroxyisobutyrylation by CobB in prokaryotes.
Dong Hanyang H Zhai Guijin G Chen Cong C Bai Xue X Tian Shanshan S Hu Deqing D Fan Enguo E Zhang Kai K
Science advances 20190717 7
Lysine 2-hydroxyisobutyrylation (Khib) has recently been shown to be an evolutionarily conserved histone mark. Here, we report that CobB serves as a lysine de-2-hydroxyisobutyrylation enzyme that regulates glycolysis and cell growth in prokaryotes. We identified the specific binding of CobB to Khib using a novel self-assembled multivalent photocrosslinking peptide probe and demonstrated that CobB can catalyze lysine de-2-hydroxyisobutyrylation both in vivo and in vitro. R58 of CobB is a critical ...[more]
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