- THIS ARTICLE
- Full Text
- Full Text (PDF)
- Alert me when this article is cited
- Alert me if a correction is posted
- SERVICES
- Similar articles in this journal
- Similar articles in PubMed
- Alert me to new issues of the journal
- Download to citation manager
- Reprints & Permissions
- CITING ARTICLES
- Citing Articles via HighWire
- Citing Articles via Google Scholar
- GOOGLE SCHOLAR
- Articles by Cheng, M. K.
- Articles by Shearn, A.
- Search for Related Content
- PUBMED
- PubMed Citation
- Articles by Cheng, M. K.
- Articles by Shearn, A.
Genetics, Vol. 167, 1213-1223, July 2004, Copyright © 2004
doi:10.1534/genetics.103.018721
The Direct Interaction Between ASH2, a Drosophila Trithorax Group Protein, and SKTL, a Nuclear Phosphatidylinositol 4-Phosphate 5-Kinase, Implies a Role for Phosphatidylinositol 4,5-Bisphosphate in Maintaining Transcriptionally Active Chromatin
Mimi K. Cheng and Allen Shearn1
Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218
1 Corresponding author: Department of Biology, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218.
E-mail: bio_cals{at}jhu.edu
The products of trithorax group (trxG) genes maintain active transcription of many important developmental regulatory genes, including homeotic genes. Several trxG proteins have been shown to act in multimeric protein complexes that modify chromatin structure. ASH2, the product of the Drosophila trxG gene absent, small, or homeotic discs 2 (ash2) is a component of a 500-kD complex. In this article, we provide biochemical evidence that ASH2 binds directly to Skittles (SKTL), a predicted phosphatidylinositol 4-phosphate 5-kinase, and genetic evidence that the association of these proteins is functionally significant. We also show that histone H1 hyperphosphorylation is dramatically increased in both ash2 and sktl mutant polytene chromosomes. These results suggest that ASH2 maintains active transcription by binding a producer of nuclear phosphoinositides and downregulating histone H1 hyperphosphorylation.
This article has been cited by other articles:
 |
|
 |
|
  J. Secombe, L. Li, L. Carlos, and R. N. Eisenman The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth Genes & Dev., March 1, 2007; 21(5): 537 - 551. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Alvarez-Venegas, M. Sadder, A. Hlavacka, F. Baluska, Y. Xia, G. Lu, A. Firsov, G. Sarath, H. Moriyama, J. G. Dubrovsky, et al. The Arabidopsis homolog of trithorax, ATX1, binds phosphatidylinositol 5-phosphate, and the two regulate a common set of target genes PNAS, April 11, 2006; 103(15): 6049 - 6054. [Abstract] [Full Text] [PDF]
|
|