Fig. 1

Full-length Asx interacts directly with SET domains of trxG activator, Trx and PcG repressor, E(z) in a GST pull-down assay. a Clustal Omega sequence alignment of SET domains of Drosophila Trx and E(z), showing 35% sequence identity. b SDS–PAGE (13%) analysis of affinity purified E. coli-expressed GST fusions of SET domains of E(z) and Trx. c GST pull-down analysis of ³⁵S-methionine-labeled rabbit reticulocyte lysate-in vitro translated (RRL-IVT) Asx with GST fusions of SET domains of E(z) and Trx. The stringency of the NaCl washes indicates stronger interaction between Asx and GST-E(z)SET than GST-TrxSET. Proteins were analyzed on 13% SDS–polyacrylamide reducing gels. ()* Estimated fold binding of Asx with GST fusions relative to GST (determined by densitometry) is shown beneath each lane