期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 99, 期 3, 页码 1241-1246出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.251672198
关键词
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资金
- NIGMS NIH HHS [R37 GM037120, GM-37120, R01 GM037120] Funding Source: Medline
A human Elongator complex was purified from HeLa cells and found to be composed of three polypeptides. Human Elongator contains histone acetyltransferase activity with specificity to histone H3 and, to a much lesser extent, to histone H4. Although many reports have suggested a role for the yeast Elongator in transcription elongation through chromatin templates, no direct evidence supporting this function exists. In the present study, we demonstrate that the human Elongator facilitates transcription by RNA polymerase II in a chromatin- and acetyl-CoA-dependent manner. The complex was found to directly interact with RNA polymerase II but failed to interact with other factors that facilitated RNA polymerase II to traverse through nucleosomes. From our results, we postulate that different mechanisms operate to ensure efficient transcription by RNA polymerase II on chromatin templates.
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