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Title 

Expression of human transglutaminase C(TGase II) in yeast Saccharomyces cerevisiae : an effect of a domain from carboxyl terminal deletion of the enzyme

 

효모시스템에서 human transglutaminase C(TGase II)의 발현에 관한 연구 : C-말단부위의 결손효과

Authors 

Sang-Kyu WooSun-Mi JungSang Ki RheeByeong-Yoon AhnHee-Chul Kim

Publisher 

Korean Journal of Applied Microbiology and Biotechnology

Issue Date 

1996

Citation 

Korean Journal of Applied Microbiology & Biotechnology, vol. 24, no. 3, pp. 290-298

Keywords 

cross-linkingtransglutaminase C (TGase II)

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 2μ-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 [1,414C]-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.

ISSN 

0257-2389

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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