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  • Title: A LexA mutant repressor with a relaxed inter-domain linker.
    Author: Oertel-Buchheit P, Reinbolt J, John M, Granger-Schnarr M, Schnarr M.
    Journal: Protein Sci; 1998 Feb; 7(2):512-5. PubMed ID: 9521130.
    Abstract:
    The LexA protein is part of a large family of prokaryotic transcriptional repressors that contain an amino-terminal DNA binding domain and a carboxy-terminal dimerization domain. These domains are separated by a linker or hinge region, which is generally considered to be rather flexible and unconstrained. So far, no structure of any of the full-length repressors is available. Here we show that a mutant LexA repressor harboring several point mutations in the hinge region gets sensitive to trypsin and Glu-C cleavage over a segment of at least 20 amino acids, whereas the LexA wild-type hinge region is resistant to these proteases. These data are not compatible with the hypothesis of an fully flexible and/or unstructured inter-domain linker and suggest that the LexA hinge region is, in fact, constrained by contacts with the carboxy-terminal domain and/or a fairly stable local structure of the linker region.
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