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. 1999 Jul;4(1):123-8.
doi: 10.1016/s1097-2765(00)80194-x.

A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme

B O Wittschieben  1 , G Otero, T de Bizemont, J Fellows, H Erdjument-Bromage, R Ohba, Y Li, C D Allis, P Tempst, J Q Svejstrup
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Free article

A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme

B O Wittschieben et al. Mol Cell. 1999 Jul.
Free article

Abstract

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 role for a novel, tightly RNAPII-associated HAT in transcription of DNA packaged in chromatin.

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