Fig. 1.
Fig. 1. Structural organization of the novel chimericMLL/AF4 transcript and protein. / (A) Analysis of the novel MLL/AF4 transcript. An RT-PCR assay was performed to evaluate whether the novelMLL/AF4 fusion gene generates a chimeric mRNA. cDNA prepared from a bone marrow RNA sample was amplified using the new primers according to sequence analysis of the panhandle product. The amplification reactions consisted of 40 cycles: 94°C, 30 seconds; 65°C, 60 seconds; and 72°C, 60 seconds. (B) Structural organization of the novel chimeric MLL/AF4 protein. The novel chimeric MLL/AF4 protein retains the DNA binding domains but lacks the AF4-derived transactivating domain, which is conserved in the usual type of this fusion protein. The junctions between the 2 protein sequences are aligned and indicated by an arrow.indicatesMLL AT hooks;,MLL repression domain;,AF4 transactivation domain; and,AF4 nuclear localization.

Structural organization of the novel chimericMLL/AF4 transcript and protein.

(A) Analysis of the novel MLL/AF4 transcript. An RT-PCR assay was performed to evaluate whether the novelMLL/AF4 fusion gene generates a chimeric mRNA. cDNA prepared from a bone marrow RNA sample was amplified using the new primers according to sequence analysis of the panhandle product. The amplification reactions consisted of 40 cycles: 94°C, 30 seconds; 65°C, 60 seconds; and 72°C, 60 seconds. (B) Structural organization of the novel chimeric MLL/AF4 protein. The novel chimeric MLL/AF4 protein retains the DNA binding domains but lacks the AF4-derived transactivating domain, which is conserved in the usual type of this fusion protein. The junctions between the 2 protein sequences are aligned and indicated by an arrow.indicatesMLL AT hooks;,MLL repression domain;,AF4 transactivation domain; and,AF4 nuclear localization.

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