Mutational Analysis of the Effector Domain of Brassica Sar1 Protein

Kim, Min-Gab; Lee, Jung-Ro; Lim, Hye-Song; Shin, Mi-Rim; Cheon, Min-Gyeong; Lee, Deok-Ho; Kim, Woe-Yeon; Lee, Sang-Yeol

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자료유형: 학술저널

저자정보: Kim, Min-Gab (Environmental Biotechnology National Core Research Center, Gyeongsang National University) Lee, Jung-Ro (Environmental Biotechnology National Core Research Center, Gyeongsang National University) Lim, Hye-Song (Environmental Biotechnology National Core Research Center, Gyeongsang National University) Shin, Mi-Rim (Environmental Biotechnology National Core Research Center, Gyeongsang National University) Cheon, Min-Gyeong (Environmental Biotechnology National Core Research Center, Gyeongsang National University) Lee, Deok-Ho (Environmental Biotechnology National Core Research Center, Gyeongsang National University) Kim, Woe-Yeon (Environmental Biotechnology National Core Research Center, Gyeongsang National University) Lee, Sang-Yeol (Environmental Biotechnology National Core Research Center, Gyeongsang National University)

저널정보: 한국응용생명화학회 Journal of applied biological chemistry Journal of applied biological chemistry 제50권 제3호

발행연도: 2007.1

수록면: 109 - 114 (6page)

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Sar1p is a ras-related GTP-binding protein that functions in intracellular protein transport between the endoplasmic reticulum (ER) and the Golgi complex. The effector domain of Ras family proteins is highly conserved and this domain is functionally interchangeable in plant, yeast and mammalian Sar1. Using a recombinant Brassica sar1 protein (Bsar1p) harboring point mutations in its effector domain, we here investigated the ability of Sar1p to bind and hydrolyze GTP and to interact with the two sar1-specific regulators, GTPase activating protein (GAP) and guanine exchange factor (GEF). The T51A and T55A mutations impaired Bsar1p intrinsic GTP-binding and GDP-dissociation activity. In contrast, mutations in the switch domain of Bsar1 did not affect its intrinsic GTPase activity. Moreover, the P50A, P54A, and S56A mutations affected the interaction between Bsar1p and GAP. P54A mutant protein did not interact with two regulating proteins, GEF and GAP, even though the mutation didn't affect the intrinsic GTP-binding, nucleotide exchange or GTPase activity of Bsar1p.

#effector domain #GAP #GEF #Mutagenesis #Sar1 GTPase

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Kim, Min-Gab

소속기관 National Academy of Agricultural Science, RDA

주요연구분야 농수해양학 > 농학

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Lee, Jung-Ro