Y. Tintut et al., RNA-POLYMERASE BINDING USING A STRONGLY ACIDIC HYDROPHOBIC-REPEAT REGION OF SIGMA(54), Proceedings of the National Academy of Sciences of the United Statesof America, 91(6), 1994, pp. 2120-2124
sigma(54) is a rare bacterial protein that substitutes for sigma(70) i
n the case of Escherichia coli genes transcribed by certain activators
with enhancer protein-like properties. It contains a strongly acidic
region of previously unknown function. Gel mobility-shift assays using
sigma(54) deletion mutants show that this region is essential for sig
ma(54) to bind the core RNA polymerase and recruit it to the promoter.
Multiple-point mutational analysis shows that the acidic amino acids
and overlapping periodic hydrophobic amino acids are necessary for thi
s binding. Related sequences are not found within the core binding det
erminant of sigma(70), which binds the same core RNA polymerase. This
comparison suggests that the core RNA polymerase interacts differently
with the two a factors, likely contributing to the critical differenc
es in transcription mechanism in the two cases.