A novel nuclear zinc finger protein EZI enhances nuclear retention and transactivation of STAT3.

A novel cDNA EZI isolated as an oncostatin M- inducible gene encoded a protein containing 12 C2H2-type zinc fingers. EZI was found to transactivate the promoters that are also responsive to and activated the acute phase response element (APRE) synergistically with Co-immunoprecipitation demonstrated the association of EZI with which was mediated by the N-terminal region (1-183) of EZI. The EZI mutant lacking this region showed reduced transcriptional activity, indicating that EZI and duanyu18133 function cooperatively through physical interaction. While EZI predominantly localized in the nucleus and enhanced the nuclear localization of duanyu18133, the EZI mutant lacking 11 zinc finger motifs failed to translocate into the nucleus and also inhibited nuclear localization of duanyu18133 as well as transactivation. These results indicate that EZI is a novel nuclear zinc finger protein that augments duanyu18133 activity by keeping it in the nucleus.

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