한빛사논문
- 조회1,777
Abstract
Yaoyao Fua,1, Youngran Kima,1, Kyeong Sik Jinb, Hyun Sook Kimc, Jong Hyun Kimd, DongMing Wanga, Minyoung Parkd, Chang Hwa Joc, Nam Hoon Kwond, Doyeun Kimd, Myung Hee Kime, Young Ho Jeonf, Kwang Yeon Hwangc,2, Sunghoon Kimd, and Yunje Choa,2
aDepartment of Life Science and
bPohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang 790-784, South Korea;
cDivision of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul 136-713, South Korea;
dMedicinal Bioconvergence Research Center, Department of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, College of Pharmacy, Seoul National University, Seoul 151-742, South Korea;
eInfection and Immunity Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, South Korea; and
fCollege of Pharmacy, Korea University, Sejong 339-700, South Korea
Abstract
In higher eukaryotes, one of the two arginyl-tRNA synthetases (ArgRSs) has evolved to have an extended N-terminal domain that plays a crucial role in protein synthesis and cell growth and in integration into the multisynthetase complex (MSC). Here, we report a crystal structure of the MSC subcomplex comprising ArgRS, glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)/p43. In this complex, the N-terminal domain of ArgRS forms a long coiled-coil structure with the N-terminal helix of AIMP1 and anchors the C-terminal core of GlnRS, thereby playing a central role in assembly of the three components. Mutation of AIMP1 destabilized the N-terminal helix of ArgRS and abrogated its catalytic activity. Mutation of the N-terminal helix of ArgRS liberated GlnRS, which is known to control cell death. This ternary complex was further anchored to AIMP2/p38 through interaction with AIMP1. These findings demonstrate the importance of interactions between the N-terminal domains of ArgRS and AIMP1 for the catalytic and noncatalytic activities of ArgRS and for the assembly of the higher-order MSC protein complex.
arginyl-tRNA synthetase, multisynthetase complex, crystal structure, AIMP1, glutaminyl-tRNA synthetase
1Y.F. and Y.K. contributed equally to this work.
2To whom correspondence may be addressed.
Author contributions: Y.F., Y.K., K.S.J., K.Y.H., and Y.C. designed research; Y.F., Y.K., K.S.J., H.S.K., J.H.K., D.W., M.P., C.H.J., and N.H.K. performed research; H.S.K. contributed new reagents/analytic tools; Y.F., Y.K., K.S.J., J.H.K., N.H.K., D.K., M.H.K., Y.H.J., K.Y.H., S.K., and Y.C. analyzed data; and S.K. and Y.C. wrote the paper.
논문정보
- Research article
- 2014년 10월 (BRIC 등록일 2014-10-13)
- 국내 연구진
- 생명과학 > 발생생물학
댓글 작성 로그인
팝업 닫기관련 링크
연구자 키워드
연구자 ID
관련분야 연구자보기
관련분야 논문보기
