CRYPTIC DNA-BINDING DOMAIN IN THE C-TERMINUS OF RNA-POLYMERASE-II GENERAL TRANSCRIPTION FACTOR RAP30
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TAN, SY
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OKLAHOMA MED RES FDN, PROGRAM MOLEC & CELL BIOL, OKLAHOMA CITY, OK 73104 USAOKLAHOMA MED RES FDN, PROGRAM MOLEC & CELL BIOL, OKLAHOMA CITY, OK 73104 USA
TAN, SY
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GARRETT, KP
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OKLAHOMA MED RES FDN, PROGRAM MOLEC & CELL BIOL, OKLAHOMA CITY, OK 73104 USAOKLAHOMA MED RES FDN, PROGRAM MOLEC & CELL BIOL, OKLAHOMA CITY, OK 73104 USA
GARRETT, KP
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CONAWAY, RC
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OKLAHOMA MED RES FDN, PROGRAM MOLEC & CELL BIOL, OKLAHOMA CITY, OK 73104 USAOKLAHOMA MED RES FDN, PROGRAM MOLEC & CELL BIOL, OKLAHOMA CITY, OK 73104 USA
CONAWAY, RC
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CONAWAY, JW
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OKLAHOMA MED RES FDN, PROGRAM MOLEC & CELL BIOL, OKLAHOMA CITY, OK 73104 USAOKLAHOMA MED RES FDN, PROGRAM MOLEC & CELL BIOL, OKLAHOMA CITY, OK 73104 USA
CONAWAY, JW
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[1] OKLAHOMA MED RES FDN, PROGRAM MOLEC & CELL BIOL, OKLAHOMA CITY, OK 73104 USA
The C terminus of mammalian transcription factor RAP30 has been found to be a cryptic DNA-binding domain strikingly similar to the C-terminal DNA-binding domain present in conserved region 4 of members of the sigma(70) family of bacterial a factors. This RAP30 domain shares strongest sequence similarity with the DNA-binding domain present in region 4 of Bacillus subtilis sporulation-specific sigma(K). Like the region 4 DNA-binding activity of Escherichia coli sigma(70) the RAP30 C-terminal DNA binding activity is masked in intact RAP30 but is readily detectable when the RAP30 C terminus is expressed as a fusion protein. Consistent with a role for RAP30 DNA-binding activity in transcription, mutations that abolish DNA binding also abolish transcription. Therefore, RAP30 may function at least in part through the action of an evolutionarily ancient DNA-binding domain that first appeared prior to the divergence of bacteria and eukaryotes.