Expression, purification and preliminary structural analysis of the head domain of Deinococcus radiodurans RecN.
Deinococcus radiodurans is well known for its extreme tolerance to harsh conditions and for its extraordinary ability to repair DNA. Double-strand breaks (DSBs) are the most hazardous lesions that can be induced by ionizing radiation, and homologous recombination (HR) is the principal mechanism by which the integrity of the DNA is restored. In D. radiodurans the RecFOR complex is the main actor in HR and the RecN protein is believed to play an important role in DSB recognition. Here, SAXS and preliminary X-ray diffraction studies are presented of the head domain, which is the globular region formed upon interaction of the N- and C-terminal domains of RecN. The crystal structure of this domain was solved using the single-wavelength anomalous dispersion method. Model building and refinement are in progress.
Structural Biology Group, European Synchrotron Radiation Facility, 6 Rue Jules Horowitz, 38043 Grenoble CEDEX 9, France.
Simone
S
Pellegrino
Jens
J
Radzimanowski
Sean
S
McSweeney
Joanna
J
Timmins
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D004262:DNA Restriction Enzymes / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D034301:Deinococcus / Q000201:enzymology*; D015870:Gene Expression; D008958:Models, Molecular; D017434:Protein Structure, Tertiary
D001426:Bacterial Proteins; D004262:DNA Restriction Enzymes; C047879:RecN protein, Bacteria