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Wada, T., Takagi, T., Yamaguchi, Y., Ferdous, A., Imai, T., Hirose, S., et al. (1998) DSIF, a Novel Transcription Elongation Factor That Regulates RNA Polymerase II Processivity, Is Composed of Human Spt4 and Spt5 Homologs. Genes & Development, 12, 343-356.
http://dx.doi.org/10.1101/gad.12.3.343

has been cited by the following article:

• TITLE: A Role for Histone Chaperones in Regulating RNA Polymerase II

  AUTHORS: JoDi Lynn Osborn, Susanna F. Greer

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

  JOURNAL NAME: Advances in Biological Chemistry, Vol.5 No.2, March 2, 2015

  ABSTRACT: 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.