Reversibly acetylated lysine residues play important roles in the enzymatic activity ofEscherichia coli N-hydroxyarylamineO-acetyltransferase

Author:

Zhang Qunfang,Gu Jing1,Gong Peng2,Wang Xude1,Tu Shun,Bi Lijun3,Yu Ziniu4,Zhang Zhiping,Cui Zongqiang,Wei Hongping,Tao Shengce,Zhang Xianen

Affiliation:

1. Key Laboratory of Agricultural and Environmental Microbiology, Wuhan Institute of Virology; Chinese Academy of Sciences; China

2. State Key Laboratory of Virology, Wuhan Institute of Virology; Chinese Academy of Sciences; China

3. National Laboratory of Biomacromolecules, Institute of Biophysics; Chinese Academy of Sciences; Beijing; China

4. State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology; Huazhong Agriculture University; Wuhan; China

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference63 articles.

1. The diversity of acetylated proteins;Polevoda;Genome Biol,2002

2. Bacterial protein acetylation: the dawning of a new age;Hu;Mol Microbiol,2010

3. Control of protein function by reversible Nε-lysine acetylation in bacteria;Thao;Curr Opin Microbiol,2011

4. Studies of the DNA binding properties of histone H4 amino terminus. Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 ‘tail’ to DNA;Hong;J Biol Chem,1993

5. Regulation of activity of the transcription factor GATA-1 by acetylation;Boyes;Nature,1998

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