Supplementary Material. Mutation of the RAD51C gene in a Fanconi anemia-like disorder
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1 Supplementary Material Mutation of the RAD51C gene in a Fanconi anemia-like disorder Fiona Vaz, Helmut Hanenberg, Beatrice Schuster, Karen Barker, Constanze Wiek, Verena Erven, Kornelia Neveling, Daniela Endt, Ian Kesterton, Flavia Autore, Franca Fraternali, Marcel Freund, Linda Hartmann, David Grimwade, Roland G Roberts, Heiner Schaal, Shehla Mohammed, Nazneen Rahman, Detlev Schindler, Christopher G Mathew
2 Supplementary Figure 1 Evolutionary conservation of R258 in the RAD51 protein family Alignment of sequences of RAD51C (RAD51L2), RAD51B (RAD51L1), RAD51 and XRCC3 from human, chicken, zebrafish, sea urchin and thale cress (Homo sapiens, Gallus gallus, Danio rerio, Strongylocentrotus purpuratus, and Arabidopsis thaliana). Secondary structure is depicted schematically above the amino acid sequences with cylinders for α-helices and arrows for β-sheets, and is taken from Shin et al (PDB 1N0W) 7 and Miller et al (Nucleic Acids Res. 32, ). The sites of the Walker B motif and the R258H mutation are indicated. (The corresponding region in RAD51D and XRCC2 seems distinct in its sequence constraints and does not contain a readily identifiable R258 counterpart).
3 Supplementary Figure 2 Maps of the retroviral vector plasmids Expression cassettes consisting of RAD51C wildtype and 773G>A mutant cdnas linked via encephalomyocarditis virus internal ribosomal entry site (IRES) to either the neomycin phosphotransferase II (nptii) gene or to the puromycin N-acetyl-transferase (pac) gene were expressed in oncoretroviral vector off the viral 5 LTR. The same viruses without RAD51C cdna were utilized as controls.
4 Supplementary Figure 3 Models of the possible structural effect of the R258H mutation in RAD51C Panels A and B show a close-up view in ribbon representation of the regions around residue 258 in wildtype arginine (A) and in mutant histidine (B) RAD51C, with loss of the interaction between H258 and the E303 carbonyl backbone. Panels C and D show the electrostatic potential surfaces of the wildtype R258 and mutant H258 RAD51C proteins respectively. The electrostatic potential surfaces have been calculated with values of the potential ranging from -6 kt (red) to the maximal positive value +6 kt (blue). The region subject to a change in the electrostatic potential from slightly positive (wildtype) to slightly negative (mutant H258) is highlighted by a square box.
5 Supplementary Table 1 Large regions of shared homozygosity in the affected siblings IV-3 and IV-5 in which the unaffected sibling was heterozygous, or homozygous for the other allele Chromosome Region of homozygosity Size (bp) to to to to to to to Supplementary Table 2 Analysis of radiosensitivity (see Online Methods) in fibroblasts from patient IV-5 (SH2038-F) before and after complementation with wildtype (wt) RAD51C. Data from cell lines from patients with known radiosensitivity are included for comparison. (ED 50 = Dose for 50% clonogenic survival; Gy = Grays) Cell line ED 50 (Gy) Control human fibroblast 1.53 SH2038-F 1.22 SH2038-F + RAD51C -wt 1.67 Ataxia telangiectasia 0.39 DNA-ligase IV deficient fibroblasts 0.61 RAD50 deficient fibroblasts 0.77
6 Supplementary Table 3 Primer sequences used to amplify and sequence RAD51C, with annealing temperature (Tm) and amplicon size (TD touchdown PCR, * indicates that DMSO was added to a final concentration of 10%). Exon Forward 5 to 3 Reverse 5 to 3 Tm ( o C) Size (bp) 1 AAATGGGATTTTGGGGAATC GTAAACATGGACGTGGGAGG TD* AAAATTAAATGGTTGATAGAATGTTGC TCAAGAAGGGATAATGAAGTAACAC GACATTTCTGTTGCCTTGGG GCTGTGGCATTTCTCATTTTG TTTTGCTATAATTTGTCATCTTTCAG TTGTAGGTCAAGGAAGGAAGAGA TTACTGTTCCAGGCATTGGG TGGAAACCAACCAAACGTAAC GTGCATGCCACCATGTCT TGTGTCTGGCCACTCAATAAA GAATAATGATTTGCAGTATTTCCC CAGACAAGGCAACAAAAGTGTC CATACGGGTAATTTGAAGGGTG TTTGGGGACAATGTTCTAAGC CGCCTGGCCCTAGAATAAA GGCCACATGAGATCAGCTTT
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