Transcriptional Elongation Factors

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  Subject Areas on Research

  • A Bayesian approach for determining protein side-chain rotamer conformations using unassigned NOE data. 
  • CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription. 
  • Expression analysis and mapping of the mouse and human transcriptional regulator CA150. 
  • Human transcription elongation factor CA150 localizes to splicing factor-rich nuclear speckles and assembles transcription and splicing components into complexes through its amino and carboxyl regions. 
  • Identification of the cellular targets of the transcription factor TCERG1 reveals a prevalent role in mRNA processing. 
  • Noncoding Transcription Is a Driving Force for Nucleosome Instability in spt16 Mutant Cells. 
  • Pol II docking and pausing at growth and stress genes in C. elegans. 
  • Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II. 
  • Retrovirus-mediated gene transfer of MLL-ELL transforms primary myeloid progenitors and causes acute myeloid leukemias in mice. 
  • Specific interaction of the transcription elongation regulator TCERG1 with RNA polymerase II requires simultaneous phosphorylation at Ser2, Ser5, and Ser7 within the carboxyl-terminal domain repeat. 
  • The elongation domain of ELL is dispensable but its ELL-associated factor 1 interaction domain is essential for MLL-ELL-induced leukemogenesis. 
  • The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1. 
  • Transcription elongation regulator 1 (TCERG1) regulates competent RNA polymerase II-mediated elongation of HIV-1 transcription and facilitates efficient viral replication. 
  • Transcriptional cofactor CA150 regulates RNA polymerase II elongation in a TATA-box-dependent manner. 
  • Use of phage display to identify novel mineralocorticoid receptor-interacting proteins. 
  • Yeast screens identify the RNA polymerase II CTD and SPT5 as relevant targets of BRCA1 interaction.