2005/08/15 by Mikael Sjölinder, Petra Björk, Emilia Söderberg +3 · 5 citations
Biochemistry, Genetics and Molecular Biology · #RNA Research and Splicing #Genomics and Chromatin Dynamics #RNA modifications and cancer #Biology #Transcription (linguistics) #Chromatin #Cell biology #Histone #Histone deacetylase 5 #Enhancer #Histone H2A #Histone deacetylase #Molecular biology #Transcription factor #Gene #Genetics
paper · pdf · doi:10.1101/gad.339405
openalex publication_date 2005/08/15 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/14
In the dipteran Chironomus tentans, actin binds to hrp65, a nuclear protein associated with mRNP complexes. Disruption of the actin-hrp65 interaction in vivo by the competing peptide 65-2CTS reduces transcription drastically, which suggests that the actin-hrp65 interaction is required for transcription. We show that the inhibitory effect of the 65-2CTS peptide on transcription is counteracted by trichostatin A, a drug that inhibits histone deacetylation. We also show that actin and hrp65 are associated in vivo with p2D10, an evolutionarily conserved protein with histone acetyltransferase activity that acts on histone H3. p2D10 is recruited to class II genes in a transcription-dependent manner. We show, using the Balbiani ring genes of C. tentans as a model system, that p2D10 is cotranscriptionally associated with the growing pre-mRNA. We also show that experimental disruption of the actin-hrp65 interaction by the 65-2CTS peptide in vivo results in the release of p2D10 from the transcribed genes, reduced histone H3 acetylation, and a lower level of transcription activity. Furthermore, antibodies against p2D10 inhibit run-on elongation. Our results suggest that actin, hrp65, and p2D10 are parts of a positive feedback mechanism that contributes to maintaining the active transcription state of a gene by recruiting HATs at the RNA level.