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PMID: 12060739 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 99 ·No. 12 ·2002-06-11 ·Pages 7912-6

Kim JY, Kang YS, Lee JW, Kim HJ, Ahn YH, Park H, Ko YG, Kim S

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.

MeSH Terms
Amino Acyl-tRNA Synthetases/chemistry,genetics,metabolism Animals Cell Line Cells, Cultured Fibroblasts/metabolism Gene Deletion Humans Kinetics Mice Mutagenesis, Site-Directed Protein Subunits Recombinant Proteins/metabolism Transcription, Genetic Transfection
Chemicals
Protein Subunits Recombinant Proteins Amino Acyl-tRNA Synthetases
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Kim Jin Young
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.
Kang Young-Sun
Lee Joong-Won
Kim Hyoung June
Ahn Young Ha
Park Heonyong
Ko Young-Gyu
Kim Sunghoon
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16 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.122110199
Published
2002-06-11
Pages
7912-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC122994
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.122110199 PMC Full Text View journal details
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