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A LexA mutant repressor with a relaxed inter‐domain linker
Author(s) -
OertelBuchheit Pascale,
Reinbolt Joseph,
Johan Matthias,
GrangerSchnarr Michèle,
Schnarr Manfred
Publication year - 1998
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560070234
Subject(s) - repressor lexa , repressor , mutant , linker , chemistry , domain (mathematical analysis) , computational biology , microbiology and biotechnology , genetics , biology , gene , computer science , transcription factor , operating system , mathematical analysis , mathematics
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.