Note Affiliated institutions 1 and 2 contributed equally to this paper.
Reversibly acetylated lysine residues play important roles in the enzymatic activity of Escherichia coli N-hydroxyarylamine O-acetyltransferase
Article first published online: 21 MAR 2013
© 2013 The Authors Journal compilation © 2013 FEBS
Volume 280, Issue 9, pages 1966–1979, May 2013
How to Cite
Zhang, Q., Gu, J., Gong, P., Wang, X., Tu, S., Bi, L., Yu, Z., Zhang, Z., Cui, Z., Wei, H., Tao, S. and Zhang, X. (2013), Reversibly acetylated lysine residues play important roles in the enzymatic activity of Escherichia coli N-hydroxyarylamine O-acetyltransferase. FEBS Journal, 280: 1966–1979. doi: 10.1111/febs.12216
- Issue published online: 25 APR 2013
- Article first published online: 21 MAR 2013
- Accepted manuscript online: 1 MAR 2013 12:39PM EST
- Manuscript Accepted: 25 FEB 2013
- Manuscript Revised: 17 FEB 2013
- Manuscript Received: 17 SEP 2012
- National Natural Science Foundation of China. Grant Numbers: 31070049, 31000388
- State Key Development Program for Basic Research of China. Grant Numbers: 2010CB529205, 2012CB518800
- National High Technology Research and Development Program of China. Grant Numbers: 2012AA020103, 2012AA020203
Vol. 280, Issue 14, 3480, Article first published online: 5 JUL 2013
Fig. S1. Full view of the E. coli proteome microarray.
Fig. S2. PCR verification of nhoA deletion in E. coli JM106 uvrA F'(CC109).
Table S1. Potential lysine-acetylated proteins from the proteome microarray.
Table S2. Primers used in this study.
Table S3. Mass spectrometry confirms that lysine 214 of NhoA is deacetylated.
Table S4. Mass spectrometry confirms that lysine 214 of NhoA is acetylated.
Table S5. Mass spectrometry confirms that lysine 281 of NhoA is deacetylated.
Table S6. Mass spectrometry confirms that lysine 281 of NhoA is acetylated.
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