Identification of a Novel Tissue-Specific Transcriptional Activator FESTA as a Protein That Interacts with the Transcription Elongation Factor S-II

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概要

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• Transcription elongation factor S-II was originally purified as a specific stimulator of transcription by RNA polymerase II. Recent studies suggest that S-II participates in gene-specific transcriptional activation in vivo, despite the fact that it directly binds RNA polymerase II and does not recognize specific DNA sequences. In this study, under the hypothesis that S-II requires co-factors to regulate the expression of specific-genes in vivo, we searched for factors that directly interact with S-II using a yeast two-hybrid system, and isolated a novel nuclear protein, FESTA. FESTA is expressed specifically in kidney and spleen, supporting our notion that S-II participates in gene-specific regulation. Two mRNA isoforms of FESTA encoding proteins with different sizes were identified and named FESTA-S and FESTA-L. FESTA contains a serine-rich region and a C-terminal tail that are highly similar to those of the ELL-associated factor EAF1. Reporter gene assays indicated that both GAL4-FESTA-S and GAL4-FESTA-L fusion proteins have trans-activating ability. Furthermore, deletion of the C-terminal tail of FESTA dramatically reduced its trans-activating ability and abolished its interaction with S-II. This study is the first report of a transcriptional activator that directly interacts with S-II and contains a transcriptional activation domain that cooperates with S-II via direct interaction.

• 社団法人 日本生化学会の論文

著者

• Sekimizu Kazuhisa

  Graduate School Of Pharmaceutical Sciences The University Of Tokyo

• Natori Shunji

  Natori Industry-sponsored Laboratory The Institute Of Physical And Chemical Research (riken)

• Saso Kayoko

  Graduate School Of Pharmaceutical Sciences University Of Tokyo

• Ito Takahiro

  Graduate School Of Electronic Science And Technology Shizuoka University

• ITO Takahiro

  Graduate School of Pharmaceutical Sciences, University of Tokyo

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