التفاصيل البيبلوغرافية
| العنوان: |
Structure and DNA-binding properties of the cytolysin regulator CylR2 from Enterococcus faecalis. |
| المؤلفون: |
Rumpel, Sigrun1, Razeto, Adelia1, Pillar, Chris M.2, Vijayan, Vinesh1, Taylor, Austin2, Giller, Karin1, Gilmore, Michael S.2, Becker, Stefan1, Zweckstetter, Markus1 mzwecks@gwdg.de |
| المصدر: |
EMBO Journal. 9/15/2004, Vol. 23 Issue 18, p3632-3642. 11p. |
| مصطلحات موضوعية: |
*ENTEROCOCCUS faecalis, *DNA-binding proteins, *ANTIBIOTICS, *BACTERIA, *BIOSYNTHESIS, *SPECTRUM analysis |
| مستخلص: |
Enterococcus faecalis is one of the major causes for hospital-acquired antibiotic-resistant infections. It produces an exotoxin, called cytolysin, which is lethal for a wide range of Gram-positive bacteria and is toxic to higher organisms. Recently, the regulation of the cytolysin operon was connected to autoinduction by a quorum-sensing mechanism involving the CylR1/CylR2 two-component regulatory system. We report here the crystal structure of CylR2 and its properties in solution as determined by heteronuclear NMR spectroscopy. The structure reveals a rigid dimer containing a helix-turn-helix DNA-binding motif as part of a five-helix bundle that is extended by an antiparallelß-sheet. We show that CylR2 is a DNA-binding protein that binds specifically to a 22 bp fragment of the cytolysin promoter region. NMR chemical shift perturbation experiments identify surfaces involved in DNA binding and are in agreement with a model for the CylR2/DNA complex that attributes binding specificity to a complex network of CylR2/DNA interactions. Our results propose a mechanism where repression is achieved by CylR2 obstruction of the promoter preventing biosynthesis of the cytolysin operon transcript. [ABSTRACT FROM AUTHOR] |
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