Akademska digitalna zbirka SLovenije - logo
VSE knjižnice (vzajemna bibliografsko-kataložna baza podatkov COBIB.SI)
  • Structural analysis of the DNA-binding domain of the Erwinia amylovora RcsB protein and its interaction with the RcsAB box
    Pristovšek, Primož ...
    The transcriptional regulator RcsB interacts with other coactivators to control the expression of biosynthetic operons in enterobacteria. While in a heterodimer complex with the regulator RcsA the ... RcsAB box consensus is recognized, DNA binding sites for RcsB without RcsA have also been identified.The conformation of RcsB might therefore be modulated upon interaction with various coactivators, resulting in the recognition of different DNA targets. We report the solution structure of the C-terminal DNA-binding domain of the RcsB protein from Erwinia amylovora spanning amino acid residues 129-215 solved by heteronuclear magnetic resonance (NMR) spectroscopy. The C-terminal domain is composed of four -helices where two central helices form a helix-turn-helix motif similar to the structures of theregulatory proteins GerE, NarL, and TraR. Amino acid residues involved in the RcsA independent DNA binding of RcsB were identified by titration studies with a RcsAB box consensus fragment. Data obtained from NMR spectroscopy together with surface plasmon resonance measurements demonstrate that the RcsAB box is specifically recognized by the RcsAB heterodimer as well as by RcsB alone. However, the binding constant of RcsB alone at target promoters from Escherichia coli, E. amylovora, and Pantoea stewartii was approximately 1order of magnitude higher compared with that of the RcsAB heterodimer. We present evidence that the obvious role of RcsA is not to alter the DNA bindingspecificity of RcsB but to stabilize RcsB-DNA complexes.
    Vir: The Journal of biological chemistry. - ISSN 0021-9258 (Vol. 278, no. 20, 2003, str. 17752-17759)
    Vrsta gradiva - članek, sestavni del
    Leto - 2003
    Jezik - angleški
    COBISS.SI-ID - 2833178

vir: The Journal of biological chemistry. - ISSN 0021-9258 (Vol. 278, no. 20, 2003, str. 17752-17759)
loading ...
loading ...
loading ...

Vnos na polico