Structural analysis of the recognition of the -35 promoter element by SigW from Bacillus subtilis
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Date
2019
Authors
Kwon, E.
Devkota, S.R.
Pathak, D.
Dahal, P.
Kim, D.Y.
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Sola, M.
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Journal article
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PLoS ONE, 2019; 14(8):e0221666-1-e0221666-13
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Eunju Kwon, Shankar Raj Devkota, Deepak Pathak, Pawan Dahal, Dong Young Kim
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Abstract
Sigma factors are key proteins that mediate the recruitment of RNA polymerase to the promoter regions of genes, for the initiation of bacterial transcription. Multiple sigma factors in a bacterium selectively recognize their cognate promoter sequences, thereby inducing the expression of their own regulons. In this paper, we report the crystal structure of the σ4 domain of Bacillus subtilis SigW bound to the -35 promoter element. Purine-specific hydrogen bonds of the -35 promoter element with the recognition helix α9 of the σ4 domain occurs at three nucleotides of the consensus sequence (G-₃₅, A-₃₄, and G’-₃₁ in G-₃₅A-₃₄A-₃₃A-₃₂ C-₃₁C-₃₀T-₂₉). The hydrogen bonds of the backbone with the α7 and α8 of the σ4 domain occurs at G’-₃₀. These results elucidate the structural basis of the selective recognition of the promoter by SigW. In addition, comparison of SigW structures complexed with the -35 promoter element or with anti-sigma RsiW reveals that DNA recognition and anti-sigma factor binding of SigW are mutually exclusive.
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© 2019 Kwon et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.