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

Jin Young Kim, Young Sun Kang, Joong Won Lee, Hyoung June Kim, Young Ha Ahn, Heonyong Park, Young Gyu Ko, Sunghoon Kim

Research output: Contribution to journalArticle

93 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)7912-7916
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume99
Issue number12
DOIs
Publication statusPublished - 2002 Jun 11

All Science Journal Classification (ASJC) codes

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