A Database of Drosophila Genes & Genomes

FB2013_03, released May 7th, 2013
 

Reference Report

Reference
Citation Labrador, M., Corces, V.G. (2003). Phosphorylation of histone H3 during transcriptional activation depends on promoter structure.  Genes Dev. 17(1): 43--48. (Export to RIS)
FlyBase ID FBrf0155495
Publication Type Research paper
PubMed ID 12514098
PubMed Abstract Covalent modifications of histone N-terminal tails are required for the proper assembly and activation of the general transcription factors at promoters. Here, we analyze histone acetylation and phosphorylation in Drosophila transgenes activated by the yeast Gal4 transcriptional activator in the context of different promoters. We show that, independent of the promoter, transcription does not correlate with acetylation of either H3-Lys 14 or H4-Lys 8. Histone H3 associated with the DNA of Gal4-induced transcribing transgenes driven by the Drosophila Hsp70 promoter is hyperphosphorylated at Ser 10 during transcription. Surprisingly, histone H3 at Gal4-induced transgenes driven by the P element Transposase promoter is not hyperphosphorylated. The data suggest that transcription occurs without acetylated H4 and H3 in both transgenes in Drosophila polytene chromosomes. Instead, phosphorylation of H3 is linked to transcription and can be modulated by the structure of the promoter.
DOI
Related Publication(s)
Personal communication to FlyBase pUAST-Hsp70:GFP4.1.3 and pUAST-Hsp70:GFP22.21.
Labrador, 2003.3.14, pUAST-Hsp70:GFP4.1.3 and pUAST-Hsp70:GFP22.21. [FBrf0155315]

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Language of Publication English
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Publication Type Journal
Abbreviation Genes Dev.
Title Genes & Development
Publication Year 1987-
ISBN/ISSN 0890-9369
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