
The research in our lab revolves around studies of the
molecular roles of post-translational modifications of proteins, and more
importantly, the mechanisms employed by these modifications to exert their
biological functions. Lee DY, Northrop JP, Kuo MH, Stallcup MR. Histone H3 lysine 9 methyltransferase G9a is a transcriptional coactivator for nuclear receptors. J Biol Chem. 2006 Mar 31;281(13):8476-85. Link to pdf
Liu, Y, Xu, X-J, Singh-Rodriguez, S, Zhao, Y, and Kuo, M-H. (2005) A histone H3 phosphorylation-independent function of Snf1 and Reg1 proteins rescues a gcn5- mutant in HIS3 expression. Mol Cell Biol. 2005 Dec;25(23):10566-79. Link to pdf
Acharya, A, Xu, X-J, Husain-Ponnampalam RD, Hoffmann-Benning S, and Kuo, M-H. (2005) Production of Constitutively Acetylated Recombinant p53 from Yeast and E. coli by Tethered Catalysis. Protein Exp. Purif. 41:417-425 Link to pdf
Guo, D., Hazbun, T., Xu, X., Ng, S-L., Fields, S., and Kuo,
M-H. (2004). A tethered catalysis two-hybrid system to identify protein-protein
interactions requiring post-translational modifications. Nature Biotechnology
(22)888-892. Link to article & sequences
Kuo, M-H. (2001). Tackling the chromatin dynamics: use of antibodies against
acetylated histones and other vibrant chromatin features. ChemTracks.
Sept;14(10)539-556.
Kuo, M-H; vom-Baur,-E; Struhl,-K; Allis,-C-D. (2000). Gcn4 activator targets
Gcn5 histone acetyltransferase to specific promoters independently of
transcription. Mol-Cell. Dec; 6(6): 1309-20.
Broday, L., W. Peng, M-H. Kuo, K. Salnikow, M. Zoroddu, and M. Costa.
(2000) Nickel compounds are novel inhibitors of histone H4 acetylation.
Can. Res. 60:238-241.
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