A unique ribonucleoprotein complex assembles preferentially on ecdysone- responsive sites in Drosophila melanogaster

S. A. Amero, M. J. Matunis, E. L. Matunis, J. W. Hockensmith, G. Raychaudhuri, A. L. Beyer

Research output: Contribution to journalArticlepeer-review

Abstract

The protein on ecdysone puffs (PEP) is associated preferentially with active ecdysone-inducible puffs on Drosophila polytene chromosomes and contains sequence motifs characteristic of transcription factors and RNA- binding proteins (S. A. Amero, S. C. R. Elgin, and A. L. Beyer, Genes Dev. 5:188-200, 1991). PEP is associated with RNA in vivo, as demonstrated here by the sensitivity of PEP-specific chromosomal immunostaining in situ to RNase digestion and by the immunopurification of PEP in Drosophila cell extract with heterogeneous nuclear ribonucleoprotein (hnRNP) complexes. As revealed by sequential immunostaining, PEP is found on a subset of chromosomal sites bound by the HRB (heterogeneous nuclear RNA-binding) proteins, which are basic Drosophila hnRNPs. These observations lead us to suggest that a unique, PEP-containing hnRNP complex assembles preferentially on the transcripts of ecdysone-regulated genes in Drosophila melanogaster presumably to expedite the transcription and/or processing of these transcripts.

Original languageEnglish (US)
Pages (from-to)5323-5330
Number of pages8
JournalMolecular and cellular biology
Volume13
Issue number9
DOIs
StatePublished - 1993

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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