Microbiology and Biotechnology Letters (한국미생물·생명공학회지)

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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효모시스템에서 Human Transglutaminase C(TGase II)의 발현에 관한 연구 : C-말단부위의 결손효과

  • 우상규 ((주)녹십자 종합연구소) ;
  • 정선미 ((주)녹십자 종합연구소) ;
  • 이상기 (한국과학기술 연구원 부설 생명공학연구소 응용미생물 연구그룹) ;
  • 안병윤 (고려대학교 자연자원대학 유전공학과) ;
  • 김희철 ((주)녹십자 종합연구소)
  • Published : 1996.06.01
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Abstract

In an effort to understand the role of the conserved domain and of the heterologous one-third part of the carboxy terminal domain of transglutaminase C (TGase II), attempts were made to express TGase II cDNA of human origin in yeast Saccharomyces cerevisiae as in a full-length form as well as in a form of C-terminal truncation. The 2$\mu$-based expression plasmids which contained the TGase II cDNA under the gal inducible promoter were introduced into yeast and the maintenance of the full-length and truncated form of the TGase II gene plasmids were confirmed by Southern blot. The expression of the TGase II gene was analysed by reverse transcription polymerase chain reaction (RT-PCR), and western blot analyses. As assayed by [1,4$^{14}$C]-putrescine incorporation into succinylated casein, the full-lenth as well as the truncated forms of recombinant TGase II showed some catalytic activity. These results indicate that the N-terminal homologous domain of human TGase II retains a catalytically active domain. The level of TGase II expressed in yeast, however, was far lower than satisfactory and other expression system should be sought further chracterization of the enzyme. The negative effect of TGase II on the growth of yeast is interesting with respect to the physiological effect of TGase II in cornification of epidermal keratinocytes.

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References

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