A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme
Research output: Contribution to journal › Journal article › Research › peer-review
The elongator complex is a major component of the RNA polymerase II (RNAPII) holoenzyme responsible for transcriptional elongation in yeast. Here we identify Elp3, the 60-kilodalton subunit of elongator/RNAPII holoenzyme, as a highly conserved histone acetyltransferase (HAT) capable of acetylating core histones in vitro. In vivo, ELP3 gene deletion confers typical elp phenotypes such as slow growth adaptation, slow gene activation, and temperature sensitivity. These results suggest a rote for a novel, tightly RNAPII-associated HAT in transcription of DNA packaged in chromatin.
| Original language | English |
|---|---|
| Journal | Molecular Cell |
| Volume | 4 |
| Issue number | 1 |
| Pages (from-to) | 123-128 |
| Number of pages | 6 |
| ISSN | 1097-2765 |
| DOIs | |
| Publication status | Published - Jul 1999 |
| Externally published | Yes |
Bibliographical note
Funding Information:
The project was supported by grants from the Imperial Cancer Research Fund and the Human Frontier Science Project (RG0193/97) to J. Q. S., by EU fellowships to B. Ø. W. and T. d. B., by a Bank of America–Giannini Foundation Medical Research Fellowship to Y. L., by an NIH grant (GM53512) to C. D. A., and by an NCI core grant (P30 CA08748) to P. T. B. Ø. W. has published previously under the name B. Ø. Petersen. We are indebted to ICRF service facilities, especially cell culture and fermentation services, for their help. A large number of colleagues, especially Alain Verrault, Rick Wood, and Brad Cairns, are thanked for their comments on the manuscript.
ID: 331575433