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SUMO Modification of NZFP Mediates Transcriptional Repression through TBP Binding
김미진,이병재,Zifan Chen,심명섭,이명숙,김지은,권영은,유택진,김진영,방제영,Bradley A. Carlson,설재홍,Dolph L. Hatfield 한국분자세포생물학회 2013 Molecules and cells Vol.35 No.1
The negatively regulating zinc finger protein (NZFP) is an essential transcription repressor required for early devel-opment during gastrulation in Xenopus laevis. In this study, we found that NZFP interacts with the small ubiq-uitin-like modifier (SUMO) conjugation E2 enzyme, Ubc9, and contains three putative SUMO conjugation sites. Studies with NZFP mutants containing mutations at the putative SUMO conjugation sites showed that these sites were able to be modified independently with SUMO. NZFP was found to be localized in the same nuclear bodies with SUMO-1. However, sumoylation of NZFP did not play a role either in the translocation of NZFP into the nucleus or on nuclear body formation. While wild type NZFP showed significant transcriptional repression, SUMO-conjugation site mutants manifested a decrease in transcriptional repression activity which is reversely proportional to the amount of sumoylation. The sumoylation defective mutant lost its TBP binding activity, while wild type NZFP interacted with TBP and inhibited transcription complex formation. These results strongly suggest that the sumoylation of NZFP facilitates NZFP to bind to TBP and the NZFP/TBP complex then represses the transcription of the target gene by in-hibiting basal transcription complex formation.
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