Expression, purification and biochemical characterization of the N-terminal regions of human TIG3 and HRASLS3 proteins

Byeong Gu Han, Jea Won Cho, Young Doo Cho, Soo Youl Kim, Hye Jin Yoon, Hyun Kyu Song, Hae Kap Cheong, Young Ho Jeon, Dong ki Lee, Sangho Lee, Byung Il Lee

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Abstract

Tarzarotene-induced gene 3 (TIG3) and HRAS-like suppressor (HRASLS3) are members of the HREV107 family of class II tumor suppressors, which are down-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 A2 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.

Original languageEnglish
Pages (from-to)103-107
Number of pages5
JournalProtein Expression and Purification
Volume71
Issue number1
DOIs
Publication statusPublished - 2010 May 1

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Keywords

  • HRASLS3
  • HREV107
  • RARRES3
  • RIG1
  • TIG3

ASJC Scopus subject areas

  • Biotechnology

Cite this

Han, B. G., Cho, J. W., Cho, Y. D., Kim, S. Y., Yoon, H. J., Song, H. K., Cheong, H. K., Jeon, Y. H., Lee, D. K., Lee, S., & Lee, B. I. (2010). Expression, purification and biochemical characterization of the N-terminal regions of human TIG3 and HRASLS3 proteins. Protein Expression and Purification, 71(1), 103-107. https://doi.org/10.1016/j.pep.2010.01.018