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Vol. 17, No. 1, pp. 43-48, January 1, 2003

RESEARCH COMMUNICATION
Phosphorylation of histone H3 during transcriptional activation depends on promoter structure

Mariano Labrador, and Victor G. Corces1

Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218, USA

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.

[Key Words: Histone; phosphorylation; acetylation; transcription; chromatin]

1 Corresponding author.

GENES & DEVELOPMENT 17:43-48 © 2003 by Cold Spring Harbor Laboratory Press  ISSN 0890-9369/03 $5.00
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