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Contributions of Distinct Quaternary Contacts to Cooperative Operator Binding by Mnt Repressor
Arie Berggrun and Robert T. Sauer
Proceedings of the National Academy of Sciences of the United States of America
Vol. 98, No. 5 (Feb. 27, 2001), pp. 2301-2305
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/3055051
Page Count: 5
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
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Mnt, a tetrameric repressor encoded by bacteriophage P22, uses N-domain dimers to contact each half of its operator site. Experiments with a double mutant and structural homology with the P22 Arc repressor suggest that contacts made by Arg-28 and stabilized by Glu-33 are largely responsible for dimer-dimer cooperativity in Mnt. These dimer-dimer contacts are energetically more important for operator binding than solution tetramerization, which is mediated by an independent C-terminal coiled-coil domain. Indeed, once one dimer of the Mnt tetramer contacts an operator half site, binding of the second dimer occurs with an effective concentration much lower than that expected if both dimers were flexibly tethered. These results suggest that binding of the second dimer introduces some strain into the protein-DNA complex, a mechanism that could serve to limit the affinity of operator binding and to prevent strong binding of the Mnt tetramer to nonoperator sites.
Proceedings of the National Academy of Sciences of the United States of America © 2001 National Academy of Sciences