کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2050058 | 1074151 | 2008 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A single residue mutation in Hha preserving structure and binding to H–NS results in loss of H–NS mediated gene repression properties
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: A single residue mutation in Hha preserving structure and binding to H–NS results in loss of H–NS mediated gene repression properties A single residue mutation in Hha preserving structure and binding to H–NS results in loss of H–NS mediated gene repression properties](/preview/png/2050058.png)
چکیده انگلیسی
In this study, we report that a single mutation of cysteine 18 to isoleucine (C18I) in Escherichia coli Hha abolishes the repression of the hemolysin operon observed in the wild-type protein. The phenotype also includes a significant decrease in the growth rate of E. coli cells at low ionic strength. Other substitutions at this position (C18A, C18S) have no observable effects in E. coli growth or hemolysin repression. All mutants are stable and well folded and bind H–NS in vitro with similar affinities suggesting that Cys 18 is not directly involved in H–NS binding but this position is essential for the activity of the H–NS/Hha heterocomplexes in the regulation of gene expression.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 582, Issue 20, 3 September 2008, Pages 3139–3144
Journal: FEBS Letters - Volume 582, Issue 20, 3 September 2008, Pages 3139–3144
نویسندگان
Tiago N. Cordeiro, Jesús Garcı´a, José-Ignacio Pons, Sonia Aznar, Antonio Juárez, Miquel Pons,