| Autor: |
P, Oertel-Buchheit, J, Reinbolt, M, John, M, Granger-Schnarr, M, Schnarr |
| Rok vydání: |
1998 |
| Předmět: |
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| Zdroj: |
Protein science : a publication of the Protein Society. 7(2) |
| ISSN: |
0961-8368 |
| Popis: |
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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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