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Genes Cells. 2003 Dec;8(12):951-61.

Carboxy-terminal region of the yeast heat shock factor contains two domains that make transcription independent of the TFIIH protein kinase.

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School of Health Sciences, Faculty of Medicine, Kanazawa University, 5-11-80 Kodatsuno, Kanazawa, Ishikawa 920-0942, Japan.



Phosphorylation of the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II is implicated in transition from initiation to elongation in the transcription cycle. In yeast cells, Kin28, a subunit of the general transcription factor TFIIH, is responsible for the CTD phosphorylation. Although Kin28 is indispensable for transcription of many genes, its requirement is bypassed in certain genes such as SSA4 or CUP1, whose transcription is activated by the heat shock factor Hsf1.


We show that C-terminal region of Hsf1, which consists of an activation domain AR2 and a regulatory domain CTM, mediates the Kin28-independent transcription. The AR2 domain, when fused to the DNA-binding domain of Gal4 and recruited to the GAL7 gene via the Gal4-binding sequence, is sufficient for activating GAL7 in the absence of Kin28. We have further found that AR2 has an ability to recruit TATA box-binding protein-associated factors (TAFs) to the promoter. Consistently, transcription from promoters occupied naturally or artificially with TAFs is sustained in the absence of Kin28 function.


These results show that CTM modulates activation function of AR2 in the Hsf1 molecule. We also suggest that recruitment of TAFs to a promoter is involved in the Kin28-independent transcription.

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