Faculty Summaries
Dr. Andrews
Andrew J. Andrews, PhD
Assistant Professor
Office Phone: 215-728-5321
Lab Phone: 215-728-3558
Office: P3133
Lab: P3117

Histone acetyltransferase specificity

• Histone chaperone mediated acetylation (Rtt109-Vps75)
• Specificity and selectivity of p300 and CBP KATs
• How acetyl-CoA concentration can alter selectivity of histone acetylation
• How chromatin dynamics influence histone acetylation

Description of research projects
Selected Publications

Fox Chase Programs

    1. Kuo, Y.M., Henry, R.A., Huang, L., Chen, X., Stargell, L.A., Andrews, A.J. Utilizing targeted mass spectrometry to demonstrate Asf1-dependent increases in residue specificity for Rtt109-Vps75 mediated histone acetylation. PLoS One 10(3), 2015 .
    3. Henry, R.A., Kuo, Y.M., Bhattacharjee, V., Yen, T.J., Andrews, A.J. Changing the selectivity of p300 by acetyl-CoA modulation of histone acetylation. ACS Chem. Biol. 10(1): 146-156, 2015.
    5. Kuo, Y.M., Henry, R.A., Andrews, A.J. A quantitative multiplexed mass spectrometry assay for studying the kinetic of residue-specific histone acetylation. Methods. 70(2-3), 127-133, 2014.
    7. Haery, L., Lugo-Picó, J.G., Henry, R.A., Andrews, A.J., Gilmore, T.D. Histone acetyltransferase-deficient p300 mutants in diffuse large B cell lymphoma have altered transcriptional regulatory activities and • are required for optimal cell growth. Mol. Cancer 13:29, 2014. PMC3930761.
    9. Kuo, Y.M., Andrews, A.J. Correction: Quantitating the specificity and selectivity of Gcn5-mediated acetylation of histone H3. PLoS One. 8(10), 2013. PMC3806868.
    11. Henry, R.A., Kuo, Y.M., Andrews, A.J. Differences in specificity and selectivity between CBP and p300 acetylation of histone H3 and H3/H4. Biochemistry 52(34):5746-59, 2013. PMC3756530.
    13. Kuo, Y.M., Andrews, A.J. Quantitating the specificity and selectivity of Gcn5-mediated acetylation of histone H3. PLoS One 8:e54896, 2013. PMC3578832.
    15. Andrews, A.J., Luger, K. Nucleosome structure(s) and stability: Variations on a theme. Annu. Rev. Biophys. 40:99-117, 2011. Review.
    17. Böhm, V., Hieb, A.R., Andrews, A.J., Gansen, A., Rocker, A., Tóth, K., Luger, K., Langowski, J. Nucleosome accessibility governed by the dimer/tetramer interface. Nucleic Acids Res. 39(8):3093-3102, 2011. PMC3082900.
    19. Andrews, A.J., Chen, X., Zevin, A., Stargell, L.A., Luger, K. The histone chaperone Nap1 promotes nucleosome assembly by eliminating nonnucleosomal histone DNA interactions. Mol. Cell 37:834-842, 2010. PMC2880918.
    20. Koutmou, K.S., Casiano-Negroni, A., Getz, M.M., Pazicni, S., Andrews, A.J., Penner-Hahn, J.E., Al-Hashimi, H.M., Fierke, C.A. NMR and XAS reveal an inner-sphere metal binding site in the P4 helix of the metallo-ribozyme ribonuclease P. Proc. Natl. Acad. Sci. USA 107:2479-2484, 2010. PMC2823894.
    21. Geiss, B.J., Thompson, A.A., Andrews, A., Sons, R.L., Gari, H.H., Keenan, S.M., Peersen, O.B. Analysis of flavivirus NS5 methyltransferase cap binding. J. Mol. Biol. 385(5):1643-1654, 2009. PMC2680092.
    22. Andrews, A., Downing, G., Brown, K., Park Y., Luger, K. A thermodynamic model for Nap1-histone interactions. J. Biol. Chem. 283(47):32412-32418, 2008. PMC2583301.
    23. Park, Y., Sudhoff, K., Andrews, A., Stargell, L., Luger, K. Histone chaperone specificity in Rtt109 activation. Nat. Struct. Mol. Biol. 15(9):957-964, 2008. PMC2680711.