Expression, purification and biochemical characterization of the N-terminal regions of human TIG3 and HRASLS3 proteins
- Authors
- Han, Byeong-Gu; Cho, Jea-Won; Cho, Young-Doo; Kim, Soo-Youl; Yoon, Hye-Jin; Song, Hyun Kyu; Cheong, Hae-Kap; Jeon, Young-Ho; Lee, Dong-Ki; Lee, Sangho; Lee, Byung Il
- Issue Date
- 5월-2010
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- TIG3; RIG1; RARRES3; HRASLS3; HREV107
- Citation
- PROTEIN EXPRESSION AND PURIFICATION, v.71, no.1, pp.103 - 107
- Indexed
- SCIE
SCOPUS
- Journal Title
- PROTEIN EXPRESSION AND PURIFICATION
- Volume
- 71
- Number
- 1
- Start Page
- 103
- End Page
- 107
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/116517
- DOI
- 10.1016/j.pep.2010.01.018
- ISSN
- 1046-5928
- Abstract
- Tarzarotene-induced gene 3 (TIG3) and HRAS-like suppressor (HRASLS3) are members of the HREV107 family of class II tumor suppressors, which are clown-regulated in various cancer cells. TIG3 and HRASLS3 also exhibit phospholipase activities. Both proteins share a common domain architecture with hydrophilic N-terminal and hydrophobic C-terminal regions. The hydrophobic C-terminal region is important for tumor suppression. However, the function of the hydrophilic N-terminal region remains elusive. To facilitate biochemical characterizations of TIG3 and HRASLS3, we expressed and purified the N-terminal regions of TIG3 and HRASLS3, designated TIG3 (1-134) and HRASLS3 (1-133), in a bacterial system. We found that the N-terminal regions of TIG3 and HRASLS3 have calcium-independent phospholipase A(2) activities. Limited proteolysis revealed that TIG3 (1-132) is a structural domain in the N-terminal region of TIG3. Our data suggest that the hydrophobic C-terminal regions might be crucial for Cellular localization, while the hydrophilic N-terminal regions are Sufficient for the enzymatic activity of both TIG3 and HRASLS3. (C) 2010 Elsevier Inc. All rights reserved.
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