Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 114, Issue 52, Pages 13661-13666Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1708563115
Keywords
histidine switch; zinc homeostasis; allostery; transcription factors; X-ray crystallography
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Funding
- National Key Research and Development Program of China [2016YFA0501500]
- National Natural Science Foundation of China [21432002, 21521003]
- E-Institutes of Shanghai Municipal Education Commission [E09013]
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Metalloregulators allosterically control transcriptional activity through metal binding-induced reorganization of ligand residues and/or hydrogen bonding networks, while the coordination atoms on the same ligand residues remain seldom changed. Here we show that the MarR-type zinc transcriptional regulator ZitR switches one of its histidine nitrogen atoms for zinc coordination during the allosteric control of DNA binding. The Zn(II)-coordination nitrogen on histidine 42 within ZitR's high-affinity zinc site (site 1) switches from N epsilon 2 to N delta 1 upon Zn(II) binding to its low-affinity zinc site (site 2), which facilitates ZitR's conversion from the nonoptimal to the optimal DNA-binding conformation. This histidine switch-mediated cooperation between site 1 and site 2 enables ZitR to adjust its DNA-binding affinity in response to a broad range of zinc fluctuation, which may allow the fine tuning of transcriptional regulation.
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