Identification and biochemical characterization of a novel transcription elongation factor, Elongin A3

K. Yamazaki, L. Guo, K. Sugahara, C. Zhang, Yusaku Nakabeppu, H. Enzan, S. Kitajima, T. Aso

研究成果: ジャーナルへの寄稿学術誌査読

25 被引用数 (Scopus)

抄録

The Elongin complex stimulates the rate of transcription elongation by RNA polymerase II by suppressing the transient pausing of the polymerase at many sites along the DNA template. Elongin is composed of a transcriptionally active A subunit and two small regulatory B and C subunits, the latter binding stably to each other to form a binary complex that interacts with Elongin A and strongly induces its transcriptional activity. To further understand the role of Elongin A in transcriptional regulation by RNA polymerase II, we are attempting to identify Elongin A-related proteins. Here, we report on the molecular cloning, expression, and biochemical characterization of human Elongin A3, a novel transcription elongation factor that exhibits 49 and 81% identity to Elongin A and the recently identified Elongin A2, respectively. The mRNA of Elongin A3 is ubiquitously expressed, and the protein is localized to the nucleus of cells. Mechanistic studies have demonstrated that Elongin A3 possesses similar biochemical features to Elongin A2. Both stimulate the rate of transcription elongation by RNA polymerase II and are capable of forming a stable complex with Elongin BC. In contrast to Elongin A, however, their transcriptional activities are not activated by Elongin BC. Structure-function analyses using fusion proteins composed of Elongin A3 and Elongin A revealed that the COOH-terminal region of Elongin A is important for the activation by Elongin BC.
本文言語英語
ページ(範囲)26444-26451
ページ数8
ジャーナルJournal of Biological Chemistry
277
29
DOI
出版ステータス出版済み - 7月 19 2002

フィンガープリント

「Identification and biochemical characterization of a novel transcription elongation factor, Elongin A3」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル