Journal article
YcgC represents a new protein deacetylase family in prokaryotes
eLife, v 4(2015)
30 Dec 2015
PMID: 26716769
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Reversible lysine acetylation is one of the most important protein posttranslational modifications that plays essential roles in both prokaryotes and eukaryotes. However, only a few lysine deacetylases (KDACs) have been identified in prokaryotes, perhaps in part due to their limited sequence homology. Herein, we developed a 'clip-chip' strategy to enable unbiased, activity-based discovery of novel KDACs in the Escherichia coli proteome. In-depth biochemical characterization confirmed that YcgC is a serine hydrolase involving Ser200 as the catalytic nucleophile for lysine deacetylation and does not use NAD(+) or Zn(2+) like other established KDACs. Further, in vivo characterization demonstrated that YcgC regulates transcription by catalyzing deacetylation of Lys52 and Lys62 of a transcriptional repressor RutR. Importantly, YcgC targets a distinct set of substrates from the only known E. coli KDAC CobB. Analysis of YcgC's bacterial homologs confirmed that they also exhibit KDAC activity. YcgC thus represents a novel family of prokaryotic KDACs.
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Details
- Title
- YcgC represents a new protein deacetylase family in prokaryotes
- Creators
- Shun Tu - Shanghai Jiao Tong UniversityShu-Juan Guo - Shanghai Jiao Tong UniversityChien-Sheng Chen - Graduate Institute of Systems Biology and Bioinformatics, National Central University, Jhongli, TaiwanCheng-Xi Liu - Shanghai Jiao Tong UniversityHe-Wei Jiang - Shanghai Jiao Tong UniversityFeng Ge - Institute of HydrobiologyJiao-Yu Deng - Wuhan Institute of VirologyYi-Ming Zhou - National Engineering Research Center for Beijing Biochip Technology, Beijing, China.Daniel M Czajkowsky - Shanghai Jiao Tong UniversityYang Li - State Key Laboratory of Oncogenes and Related Genes, Shanghai, ChinaBang-Ruo Qi - Shanghai Jiao Tong UniversityYoung-Hoon Ahn - Johns Hopkins University School of MedicinePhilip A Cole - Johns Hopkins MedicineHeng Zhu - Johns Hopkins MedicineSheng-Ce Tao - Shanghai Jiao Tong University
- Publication Details
- eLife, v 4(2015)
- Publisher
- eLife
- Grant note
- R37 GM062437 / NIGMS NIH HHS R01 AA020203 / NIAAA NIH HHS U54 HG006434 / NHGRI NIH HHS R01 GM111514 / NIGMS NIH HHS GM076102 / NIGMS NIH HHS R01 GM076102 / NIGMS NIH HHS GM62437 / NIGMS NIH HHS R01 AA020103 / NIAAA NIH HHS R01 GM062437 / NIGMS NIH HHS RR020839 / NCRR NIH HHS U54 RR020839 / NCRR NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- College of Arts and Sciences; Chemistry; Drexel University
- Web of Science ID
- WOS:000367517800001
- Scopus ID
- 2-s2.0-84962408286
- Other Identifier
- 991020099992004721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biology