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- W2029793889 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." @default.
- W2029793889 created "2016-06-24" @default.
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- W2029793889 date "1998-02-01" @default.
- W2029793889 modified "2023-10-18" @default.
- W2029793889 title "A LexA mutant repressor with a relaxed inter-domain linker" @default.
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- W2029793889 doi "https://doi.org/10.1002/pro.5560070234" @default.
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