TY - JOUR
T1 - Identification of a yeast transcription factor IID subunit, TSG2/TAF48
AU - Reese, Joseph C.
AU - Zhang, Zhengjian
AU - Kurpad, Harsha
PY - 2000/6/9
Y1 - 2000/6/9
N2 - The RNA polymerase II general transcription factor TFIID is a complex containing the TATA-binding protein (TBP) and associated factors (TAFs). We have used a mutant allele of the gene encoding yeast TAF(II)68/61(p) to analyze its function in vivo. We provide biochemical and genetic evidence that the C-terminal α-helix of TAF(II)68/61p is required for its direct interaction with TBP, the stable incorporation of TBP into the TFIID complex, the integrity of the TFIID complex, and the transcription of most genes in vivo. This is the first evidence that a yeast TAF(II) other than TAF(II)145/130 inter acts with TBP, and the implications of this on the interpretation of data obtained studying TAF(II) mutants in vivo are discussed. We have identified a high copy suppressor of the TAF68/61 mutation, TSG2, that has sequence similarity to a region of the SAGA subunit Ada1. We demonstrate that it directly interacts with TAF(II)68/61p in vitro, is a component of TFIID, is required for the stability of the complex in vivo, and is necessary for the transcription of many yeast genes. On the basis of these functions, we propose that Tsg2/TAF(II)48(p) is the histone 2A-like dimerization partner for the histone 2B-like TAF(II)68/61(p) in the yeast TFIID complex.
AB - The RNA polymerase II general transcription factor TFIID is a complex containing the TATA-binding protein (TBP) and associated factors (TAFs). We have used a mutant allele of the gene encoding yeast TAF(II)68/61(p) to analyze its function in vivo. We provide biochemical and genetic evidence that the C-terminal α-helix of TAF(II)68/61p is required for its direct interaction with TBP, the stable incorporation of TBP into the TFIID complex, the integrity of the TFIID complex, and the transcription of most genes in vivo. This is the first evidence that a yeast TAF(II) other than TAF(II)145/130 inter acts with TBP, and the implications of this on the interpretation of data obtained studying TAF(II) mutants in vivo are discussed. We have identified a high copy suppressor of the TAF68/61 mutation, TSG2, that has sequence similarity to a region of the SAGA subunit Ada1. We demonstrate that it directly interacts with TAF(II)68/61p in vitro, is a component of TFIID, is required for the stability of the complex in vivo, and is necessary for the transcription of many yeast genes. On the basis of these functions, we propose that Tsg2/TAF(II)48(p) is the histone 2A-like dimerization partner for the histone 2B-like TAF(II)68/61(p) in the yeast TFIID complex.
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U2 - 10.1074/jbc.M001635200
DO - 10.1074/jbc.M001635200
M3 - Article
C2 - 10751405
AN - SCOPUS:0034625404
VL - 275
SP - 17391
EP - 17398
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 23
ER -