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¹ Graduate School of Frontier Biosciences, and ² Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka 565-0871, Japan
³ Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Suita, Osaka 565-0871, Japan
⁴ Cellular Physiology Laboratory, RIKEN, Wako, Saitama 351-0198, Japan
⁵ Gene Engineering Division, BioResource Center, RIKEN, Tsukuba, Ibaraki 305-0074, Japan
⁶ Nippon Institute for Biological Science, Ome, Tokyo 190-0024, Japan

The general transcription factor TFIIE plays essential roles in transcription by RNA polymerase II (PolII). Despite recent progress, the elucidation of its precise mechanisms including biological functions awaits further characterization. We report the isolation and characterization of Schizosaccharomyces pombe TFIIE (spTFIIE). Like human and other eukaryotic TFIIE proteins, spTFIIE consists of and ß subunits and the genes encoding both subunits are essential for viability. Chromatin immunoprecipitation assays demonstrated that spTFIIE localizes to promoters in vivo. Mutational analysis of the C-terminal basic helix-loop region of TFIIEß, which is involved in the transition from transcription initiation to elongation, revealed that transcription-defective mutants affected in this region are also cold sensitive. The spTFIIEß subunit binds both spTFIIEß and spTFIIE but spTFIIE binds only spTFIIEß. These results indicate that TFIIE forms an ₂ß₂ heterotetramer in which two ß heterodimers are connected via ß subunits. Further analysis of binding specificities showed that spTFIIEß binds the Rpb2 and Rpb12 subunits of PolII, whereas spTFIIE predominantly binds Rpb5, which is located at the clamp region and changes conformation upon transcription initiation.

^aPresent address: Discovery Research Laboratories II, Pharmaceutical Research Division, Takeda Chemical Industries Ltd, Tsukuba, Ibaraki 300-4247, Japan

^bPresent address: Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-0194, Japan

^* Correspondence: E-mail: ohkumay{at}ms.toyama-mpu.ac.jp

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