| Brpf1 is an important member of TrxG family, which contains C2H2,PHD,Bromodomain and PWWP domains, and it plays considerable role in transcription and translation processes. But Brpf2 is a novel transcript of Brpf1, which has only C2H2 and PHD domains, premature transcription termination on account of clipping selectivity. Up to now, there have not research about it to be shown. Our laboratory previously confimed the expression map of Brpf1 and Brpf2 mRNA.In this research, we detected proterin distribution of Brpf1 and Brpf2 in defferent tissue and predicted their structures and functions by variously bioinformatics.By western blotting test, Brpf1 and Brpf2 proteins were identified in 9 different tissues, testis, epididymis, heart, hepar, spleen, kidney, embryo, ovary and uterus. Bio informatics methods were used to analyze Brpf1 and Brpf2's secondary structure, solvents accessibility, functional sites and transmembrane region, and predict tertiary structure. Results showed Brpfl displayed a 'β-barrel' structure, while Brpf2 contained many connected hairpins, neither of which had transmembrane regions, and these two proteins had different potential functional sites for DNA binding, acetylation, methylation and phosphorylation.In the preceding yeast two-hybrid experiment, which is accomplished in common, the interaction between Brpf1, Brpf2 and Rhox5 and their capital domains are demonstrated. This research confirmed the interaction between Brpf1, Brpf2 and Rhox5 and their capital domains by means of fluorescent co-localization. Results showed that, in mammalian cells, Brpf2 interacted with Rhox5, for which the PHD domain of Brpf2 is indispensable, however, Brpfl did not bind with Rhox5, although it contained two PHD domains.To explore Brpf1 and Brpf2's fuctions further, NIH3T3 cell lines was constructed to stably express Brpf1 and Brpf2, repspetively. And Brpf1 and Brpf2 proteins expressed in prokaryotic cells were purified successfully.
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