Journal
NATURE REVIEWS MICROBIOLOGY
Volume 5, Issue 9, Pages 710-720Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nrmicro1717
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Funding
- NATIONAL CENTER FOR RESEARCH RESOURCES [P20RR016439] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM069857] Funding Source: NIH RePORTER
- NCRR NIH HHS [RR016439] Funding Source: Medline
- NIGMS NIH HHS [R01 GM069857, GM69857] Funding Source: Medline
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The ribbon-helix-helix (RHH) superfamily of transcription factors uses a conserved three-dimensional structural motif to bind to DNA in a sequence-specific manner. This functionally diverse protein superfamily regulates the transcription of genes that are involved in the uptake of metals, amino-acid biosynthesis, cell division, the control of plasmid copy number, the lytic cycle of bacteriophages and, perhaps, many other cellular processes. In this Analysis, the structures of different RHH transcription factors are compared in order to evaluate the sequence motifs that are required for RHH-domain folding and DNA binding, as well as to identify conserved protein-DNA interactions in this superfamily.
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