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A Novel Glycine-Rich Region in Sox4 is a Target for the Proteolytic Cleavage in E. coli  

허은혜 (가톨릭대학교 이과학연구원 분자유전학연구소, 가톨릭대학교 의과대학 생화학교실)
최주연 (가톨릭대학교 이과학연구원 분자유전학연구소, 상명대학교 생물학과)
장경희 (가톨릭대학교 이과학연구원 분자유전학연구소)
김인경 (가톨릭대학교 이과학연구원 분자유전학연구소, 가톨릭대학교 의과대학 생화학교실)
임향숙 (가톨릭대학교 이과학연구원 분자유전학연구소)
Publication Information
Korean Journal of Microbiology / v.38, no.3, 2002 , pp. 153-161 More about this Journal
Abstract
Sox4, a transcription factor, consists of three functional domains: an HMG-box domain as a DNA binding domain, serine rich region as a transactivation domain and glycine rich region (GRR), an unknown functional domain. Although Sox4 is known to be functionally involved in heart, B-cell and reproductive system development, its physiological function remains to be elucidated. We used pGEX expression system to develop a simple and rapid method for purifying Sox4 protein in suitable forms for biochemical studies of their functions. Unexpectedly, we observed that full-length Sox4 appears to be protease-sensitive during expression and purification in E. coli. To map the protease-sensitive site in Sox4, we generated various constructs with each of functional domains of Sox4 and purified as the GST-Sox4 fusion proteins using glutathione beads. We found that the specific cleavage site for the proteolytic enzyme, which exists in E. coli, is localized within the novel GRR of Sox4. Our study suggest that the GRR of Sox4 may a target for the cellular protease action and this cleavage in the GRR may be involved in regulating physiological function of Sox4. Additionally, our study may provide a useful method for investigating the proteolytic cleavage of the target molecule in E. coli.
Keywords
GRR; GST-Sox4; protease-sensitivity;
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