THE TRANSLATION PRODUCT OF THE PRESUMPTIVE THERMOCOCCUS-CELER TATA-BINDING PROTEIN-SEQUENCE IS A TRANSCRIPTION FACTOR-RELATED IN STRUCTURE AND FUNCTION TO METHANOCOCCUS TRANSCRIPTION FACTOR-B
W. Hausner et M. Thomm, THE TRANSLATION PRODUCT OF THE PRESUMPTIVE THERMOCOCCUS-CELER TATA-BINDING PROTEIN-SEQUENCE IS A TRANSCRIPTION FACTOR-RELATED IN STRUCTURE AND FUNCTION TO METHANOCOCCUS TRANSCRIPTION FACTOR-B, The Journal of biological chemistry, 270(30), 1995, pp. 17649-17651
A gene for a putative homolog of TATA-binding protein (TBP) from Therm
ococcus celer has been expressed in Escherichia coli, and the function
of the purified recombinant protein was studied in a Methanococcus-de
rived cell-free transcription system. Thermococcus TBP can replace arc
haeal transcription factor B (aTFB) in cell-free transcription reactio
ns. This transcriptional activation is TATA box-dependent and occurs b
oth on tRNA(Val) and protein-encoding genes as templates indicating th
at Thermococcus TBP is a general transcription factor. Antibodies rais
ed against Thermococcus TBP bind to Methanococcus aTFB and inhibit aTF
B activity. These findings demonstrate that Thermococcus TBP (like euc
aryal TBPs) can direct specific transcription from TATA boxes.