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. 2009 Mar 30;284(23):15701–15707. doi: 10.1074/jbc.M808431200

FIGURE 1.

FIGURE 1.

HnRNP-L is a novel subunit of the human KMT3a complex. A, domain structure of human KMT3a and yeast KMT3. B, silver staining indicates co-elution of HnRNP-L with FLAG -KMT3a-C. Fractions were from a 2-ml Smart Superose 6 gel filtration column. The input of this column is affinity-purified KMT3a from cells stably expressing FLAG-KMT3a-C. Fraction numbers are shown at the top of the panel. C, interaction between KMT3a and HnRNP-L is independent of RNase treatment. D, endogenous, full-length KMT3a co-purifies with FLAG-HnRNP-L in nuclear extracts from stable cells expressing FLAG-HnRNP-L. E, reciprocal co-immunoprecipitation experiments demonstrate interactions between endogenous KMT3a and HnRNP-L in HeLa cells.