p38 is essential for the assembly and stability of macromolecular tRNA synthetase complex: implications for its physiological significance.

Kim JinYoung; Kang YoungSun; Lee JoongWonKim HyoungJuneAhn YoungHaPark HeonyongKo YoungGyuKim Sunghoon

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p38 is essential for the assembly and stability of macromolecular tRNA synthetase complex: implications for its physiological significance.

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Mammalian tRNA synthetases form a macromolecular complex with three nonenzyme factors: p43, p38, and p18. Here we introduced a mutation within the mouse p38 gene to understand its functional significance for the formation of the multi-tRNA synthetase complex. The complex was completely disintegrated by the deficiency of p38. In addition, the protein levels and catalytic activities of the component enzymes and cofactors were severely decreased. A partial truncation of the p38 polypeptide separated the associated components into different subdomains. The mutant mice showed lethality within 2 days of birth. Thus, this work provides the first evidence, to our knowledge, that p38 is essential for the structural integrity of the multi-tRNA synthetase complex and mouse viability.

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《Proceedings of the National Academy of Sciences of the United States of America》 |2002年第12期|7912-7916|共5页
作者
Kim JinYoung; Kang YoungSun; Lee JoongWonKim HyoungJuneAhn YoungHaPark HeonyongKo YoungGyuKim Sunghoon;
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作者单位

National Creative Research Initiatives Center for ARS Network, College of Pharmacy, Seoul National University, San 56-1, Shillim-dong, Kwanak-gu, Seoul 151-746, Korea.;

heasant.pharm.okayama-u.ac.jp;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
Amino Acyl tRNA Ligases genetics; Amino Acyl tRNA Ligases metabolism; Protein Subunits;

p38 is essential for the assembly and stability of macromolecular tRNA synthetase complex: implications for its physiological significance.

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