The RNA polymerase II molecule at the 5' end of the uninduced hsp70 gene of D. melanogaster is transcriptionally engaged

Cell. 1988 Sep 9;54(6):795-804. doi: 10.1016/s0092-8674(88)91087-2.


Protein-DNA cross-linking of cultured Drosophila cells has shown that, in vivo, prior to the induction of heat shock, there is approximately one molecule of RNA polymerase II associated with the promoter region of the major heat shock gene, hsp70. Here, we show that this promoter-associated RNA polymerase II molecule is transcriptionally engaged and has formed a nascent RNA chain of approximately 25 nucleotides in length, but is apparently arrested at that point and unable to penetrate further into the hsp70 gene without heat induction. The detection of a post-initiation RNA polymerase complex on the promoter region of the inactive gene suggests that there is a transcriptional control mechanism that acts at a step early in transcript elongation.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Base Sequence
  • Cell Nucleus / metabolism
  • Drosophila melanogaster
  • Gene Expression Regulation*
  • Heat-Shock Proteins / genetics*
  • In Vitro Techniques
  • RNA Polymerase II / metabolism*
  • Regulatory Sequences, Nucleic Acid*
  • Transcription Factors / physiology
  • Transcription, Genetic*


  • Heat-Shock Proteins
  • Transcription Factors
  • RNA Polymerase II