Author(s)

JoDi Lynn Osborn, Susanna F. Greer^*

Department of Biology, Georgia State University, Atlanta, USA.

Transcription is a highly regulated cellular process in which dysfunction leads to disease. One level of regulation is chromatin structure which protects promoters from transcription factor binding. To circumvent this blockade, histone chaperones aid in displacement of nucleosomes. In particular, the histone chaperone complex HUCA, consisting of Hira, Ubn1, Cabin1, and ASF1a, replaces histone variant H3.1 with H3.3 in front of actively transcribing RNA Polymerase II (RNAPII). The 26S proteasome is a major degrader of proteins within the cell and plays both proteolytic and non- proteolytic roles in transcriptional regulation. One major role is the degradation of irreversibly arrested RNAPII. Several interactions between HUCA, the 26S proteasome, and RNAPII have been characterized individually; we now present observations from our lab and others which directly associate elongating RNAPII with the degradation machinery through observations of involvement with the HUCA complex. Our short report presents these ideas and discusses their importance in transcriptional regulation as well as implications in disease manifestation.

Histone Chaperones, RNA Polymerase II, 26S Proteasome, Transcriptional Regulation

Osborn, J. and Greer, S. (2015) A Role for Histone Chaperones in Regulating RNA Polymerase II. Advances in Biological Chemistry, 5, 35-44. doi: 10.4236/abc.2015.52004.