Reversibly acetylated lysine residues play important roles in the enzymatic activity ofEscherichia coli N-hydroxyarylamineO-acetyltransferase-Reference-Cited by-同舟云学术

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

Published:2013-03-21 Issue:9 Volume:280 Page:1966-1979
ISSN:1742-464X
Container-title:FEBS Journal
language:en
Short-container-title:FEBS J

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

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/febs.12216/fullpdf

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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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