Fig. 7.
Fig. 7. The GATA-1C–finger secondary structure is not required for interaction with PU.1. / (A) In vitro–translated 35S-labeled PU.1 and N-terminal deletion mutant input proteins (3 μL). Lane 1: PU.1; lane 2: PUDN56; lane 3: PUDN100; lane 4: PUDN143. (B) Pulldown of35S-labeled PU.1 proteins (5 μL) with GST-GATA-1 fusions. Lanes 1-4 as in (A). (C) Pulldown as in (B) with GST fusion containing the wild-type GATA-1 finger region (GST-G1 NF+CF wt). (D) Pulldown as in (B) with GST fusion of GATA-1 finger region carrying point mutations in the N-finger (GST-G1 NF+CF mutNF). (E) Pulldown as in (B) with GST fusion of GATA-1 finger region carrying point mutations in the C-finger (GST-G1 NF+CF mutCF).

The GATA-1C–finger secondary structure is not required for interaction with PU.1.

(A) In vitro–translated 35S-labeled PU.1 and N-terminal deletion mutant input proteins (3 μL). Lane 1: PU.1; lane 2: PUDN56; lane 3: PUDN100; lane 4: PUDN143. (B) Pulldown of35S-labeled PU.1 proteins (5 μL) with GST-GATA-1 fusions. Lanes 1-4 as in (A). (C) Pulldown as in (B) with GST fusion containing the wild-type GATA-1 finger region (GST-G1 NF+CF wt). (D) Pulldown as in (B) with GST fusion of GATA-1 finger region carrying point mutations in the N-finger (GST-G1 NF+CF mutNF). (E) Pulldown as in (B) with GST fusion of GATA-1 finger region carrying point mutations in the C-finger (GST-G1 NF+CF mutCF).

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