Fig. 1.
Fig. 1. The FAA-GFP chimera complements MMC-hypersensitivity in FA-A lymphoblasts. (A) Schematic representation of FAA-GFP. Indicated are the relative positions of both the putative bipartite nuclear localization domain (NLS) and leucine repeat motif (L-zip.). The cloning strategy used resulted in the insertion of 13 amino acids (aa), KLDIEFLQPGGST, leading to a hybrid protein encompassing 1,706 aa with a molecular weight of approximately 190 kD. (B) MMC-dependent growth inhibition in stably transfected HSC72 (FA-A) cells. The expression vector pDR2 alone or containing the GFP, FAA, or FAA-GFP coding regions were stably transfected in HSC72 cells and MMC-complementing activity of the constructs was determined.

The FAA-GFP chimera complements MMC-hypersensitivity in FA-A lymphoblasts. (A) Schematic representation of FAA-GFP. Indicated are the relative positions of both the putative bipartite nuclear localization domain (NLS) and leucine repeat motif (L-zip.). The cloning strategy used resulted in the insertion of 13 amino acids (aa), KLDIEFLQPGGST, leading to a hybrid protein encompassing 1,706 aa with a molecular weight of approximately 190 kD. (B) MMC-dependent growth inhibition in stably transfected HSC72 (FA-A) cells. The expression vector pDR2 alone or containing the GFP, FAA, or FAA-GFP coding regions were stably transfected in HSC72 cells and MMC-complementing activity of the constructs was determined.

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