PROFILING PROTEIN INTERACTIONS OF H33, H32, AND H31

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. We studied the H3 proteins using our approach for the rapid and efficient isolation of a GFP-tagged protein with its interacting partners. Our first experiments focused on the H3.3 variant, and we optimized the lysis and isolation conditions for the purification of this protein via a GFP tag. The results were published: Distinct factors control histone variant H3.3 localization at specific genomic regions. Goldberg AD, Banaszynski LA, Noh KM, Lewis PW, Elsaesser SJ, Stadler S, Dewell S, Law M, Guo X, Li X, Wen D, Chapgier A, DeKelver RC, Miller JC, Lee YL, Boydston EA, Holmes MC, Gregory PD, Greally JM, Rafii S, Yang C, Scambler PJ, Garrick D, Gibbons RJ, Higgs DR, Cristea IM, Urnov FD, Zheng D, Allis CD. Cell. 2010 Mar 5;140(5):678-91.