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제117회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Crystallization of Ate1, arginyl tRNA protein transferase 1 from yeast

2016년 2월 25일 15시 15분 22초
BIO.P-313 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
4월 21일 (목요일) 11:00~12:30
저자 및
오선주, 김민경1, 송현규1,*
고려대학교 생명과학과, Korea
1고려대학교 생명과학부, Korea
N-end rule is one of the protein degradation pathways occurring in mammals, yeast and plant cells [1]. It has been reported that there are two different types of pathway, Ac/N-end and Arg/N-end rule. In the Ac/N-end pathway, N-terminally acetylated residues of the target protein are recognized by the membrane-bound E3-ubiquitin ligase, Doa10. In the Arg/N-end rule pathway, the arginine (or lysine, histidine) residue of the target protein is recognized by Ubr1 E3 ligase. There are hierarchical steps, which are initiated by deamination of N-terminal asparagine or glutamine residue by Nat1. Next, Ate1, arginyl-tRNA-protein transferase adds arginine to the N-terminal aspartate or glutamate residue [2]. Finally the N-degron bearing arginine is recognized by the Ubr1 E3-ubiquitin ligase and subsequently degraded by the 26S proteasome. Until now, the Rgs4, Rgs5, Rgs16 regulators of G proteins and BiP/GRP78 molecular chaperone are identified as physiological substrates of Ate1. The Ate1 plays a critical role in various cellular processes including embryogenesis, cell migration, and muscle contraction. However, the enzymatic mechanism of Ate1 remains unclear due to the lacking of its structural information. As a first step toward structural study of Ate1, we over-expressed Ate1 proteins from yeast species, Kluyveromyces lactis using C-terminal 6-histidine-tag in E.coli. Ate1 proteins are successfully purified as homogeneity and crystallization trial is underway.