Albany 2013: Book of Abstracts
June 11-15 2013
©Adenine Press (2012)
NMR study of RQC domain of BLM protein
BLM, a member of the RecQ helicase associated with the Bloom’s syndrome human genetic disorder, has been found to bind to non canonical DNA with high affinity via its RecQ C-terminal domain (RQC). Using multi-dimensional NMR spectroscopy, we have determined the solution structure of BLM RQC, and found that BLM RQC retains the overall winged-helix motif previously observed for other RQC proteins. Comparison between BLM RQC and the RQC domain of its homologue, Werner syndrome protein (WRN RQC), revealed two major structural differences. Firstly, BLM RQC contains an extended 14-residue insertion forming a flexible loop between two first α-helices, only found in BLM RQC and not other RQC proteins. Secondly, in contrast to the third α-helix of WRN RQC, an unstructured loop was observed for this region of BLM RQC.