Journal
NATURE CHEMICAL BIOLOGY
Volume 17, Issue 1, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41589-020-00653-x
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Funding
- National Key Research and Development Program of China [2018YFA0900701, 2018YFA0507800]
- Strategic Priority Research Program of CAS [XDB29020000]
- National Natural Science Foundation of China [31822001, 31970040]
- Leading Science Key Research Program of CAS [QYZDB-SSW-SMC005]
- National Institutes of Health of the United States [GM038784-31, CA193419]
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MerR family transcription factors are able to reshape promoter DNA through clamp-like protein-DNA interactions, promoting productive promoter-polymerase association without canonical protein-protein contacts seen in other activator proteins. These structural and biochemical findings strongly support the DNA distortion paradigm for allosteric transcriptional control by MerR TFs.
The MerR-family transcription factors (TFs) are a large group of bacterial proteins responding to cellular metal ions and multiple antibiotics by binding within central RNA polymerase-binding regions of a promoter. While most TFs alter transcription through protein-protein interactions, MerR TFs are capable of reshaping promoter DNA. To address the question of which mechanism prevails, we determined two cryo-EM structures of transcription activation complexes (TAC) comprisingEscherichia coliCueR (a prototype MerR TF), RNAP holoenzyme and promoter DNA. The structures reveal that this TF promotes productive promoter-polymerase association without canonical protein-protein contacts seen between other activator proteins and RNAP. Instead, CueR realigns the key promoter elements in the transcription activation complex by clamp-like protein-DNA interactions: these induce four distinct kinks that ultimately position the -10 element for formation of the transcription bubble. These structural and biochemical results provide strong support for the DNA distortion paradigm of allosteric transcriptional control by MerR TFs.
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