Skip Navigation


Radiation Protection Dosimetry Advance Access originally published online on January 17, 2007
Radiation Protection Dosimetry 2006 122(1-4):100-105; doi:10.1093/rpd/ncl442
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
122/1-4/100    most recent
ncl442v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Davídková, M.
Right arrow Articles by Spotheim-Maurizot, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Davídková, M.
Right arrow Articles by Spotheim-Maurizot, M.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2006. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

INVITED PAPER

Modification of DNA radiolysis by DNA-binding proteins: structural aspects

Marie Davídková1,*, Viktorie Stísová1,3, Stephane Goffinont2, Nathalie Gillard2, Bertrand Castaing2 and Melanie Spotheim-Maurizot2

1 Department of Radiation Dosimetry, Nuclear Physics Institute AS CR, Na Truhlárce 39/64, 180 86, Praha 8, Czech Republic
2 Centre de Biophysique Moléculaire CNRS, rue Charles Sadron, 45100 Orléans Cedex 2, France
3 Department of Dosimetry and Application of Ionizing Radiation, Faculty of Nuclear Sciences and Physical Engineering, CTU Prague, Brehová 7, 115 19, Praha 1, Czech Republic

* Corresponding author: davidkova{at}ujf.cas.cz


   Abstract

Formation of specific complexes between proteins and their cognate DNA modulates the yields and the location of radiation damage on both partners of the complex. The radiolysis of DNA–protein complexes is studied for: (1) the Escherichia coli lactose operator–repressor complex, (2) the complex between DNA bearing an analogue of an abasic site and the repair protein Fpg of Lactococcus lactis. Experimental patterns of DNA damages are presented and compared to predicted damage distribution obtained using an improved version of the stochastic model RADACK. The same method is used for predicting the location of damages on the proteins. At doses lower than a threshold that depends on the system, proteins protect their specific binding site on DNA while at high doses, the studied complexes are disrupted mainly through protein damage. The loss of binding ability is the functional consequence of the amino-acids modification by OH· radicals. Many of the most probably damaged amino acids are essential for the DNA–protein interaction and within a complex are protected by DNA.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.