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"DNA end-binding specificity of human Rad50/Mre11 is influenced by ATP." |
de Jager M, Wyman C, van Gent DC, Kanaar R |
Published Oct. 15, 2002 in Nucleic Acids Res volume 30 .
Pubmed ID: 12384589
Abstract:
| The Rad50, Mre11 and Nbs1 complex is involved in many essential chromosomal organization processes dealing with DNA ends, including two major pathways of DNA double-strand break repair, homologous recombination and non-homologous end joining. Previous data on the structure of the human Rad50 and Mre11 (R/M) complex suggest that a common role for the protein complex in these processes is to provide a physical link between DNA ends such that they can be processed in an organized and coordinated manner. Here we describe the DNA binding properties of the R/M complex. The complex bound to both single-stranded and double-stranded DNA. Scanning force microscopy analysis of DNA binding by R/M showed the requirement for an end to form oligomeric R/M complexes, which could then migrate or transfer away from the end. The R/M complex had a lower preference for DNA substrates with 3'-overhangs compared with blunt ends or 5'-overhangs. Interestingly, ATP binding, but not hydrolysis, increased the preference of R/M binding to DNA substrates with 3'-overhangs relative to substrates with blunt ends and 5'-overhangs. |
This publication refers to following REPAIRtoire entries:
| Proteins |
Last modification of this entry: Oct. 6, 2010
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