Fig. 6.
Fig. 6. The ETS domain of PU.1 is required for interaction with GATA-1. / (A) The structure of the PUDC198 protein, in which most of the ETS domain has been deleted. (B) Wild-type PU.1 and PUDC198 were35S-labeled by in vitro translation, and 4-μL aliquots were separated on a 12% SDS-PAGE gel and detected by phosphorimaging. (C) Four-microliter 35S-labeled PU.1 (upper panel) and PUDC198 (lower panel) proteins were subjected to GST pulldown analysis and bound proteins detected as in Figure 5D.

The ETS domain of PU.1 is required for interaction with GATA-1.

(A) The structure of the PUDC198 protein, in which most of the ETS domain has been deleted. (B) Wild-type PU.1 and PUDC198 were35S-labeled by in vitro translation, and 4-μL aliquots were separated on a 12% SDS-PAGE gel and detected by phosphorimaging. (C) Four-microliter 35S-labeled PU.1 (upper panel) and PUDC198 (lower panel) proteins were subjected to GST pulldown analysis and bound proteins detected as in Figure 5D.

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