Solution structure and p43 binding of the p38 leucine zipper motif: Coiled-coil interactions mediate the association between p38 and p43

Hee Chul Ahn, Sunghoon Kim, Bong Jin Lee

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

p38, which has been suggested to be a scaffold protein for the assembly of a macromolecular tRNA synthetase complex, contains a leucine zipper-like motif. To understand the importance of the leucine zipper-like motif of p38 (p38LZ) in macromolecular assembly, the p38LZ solution structure was investigated by circular dichroism and nuclear magnetic resonance spectroscopy. The solution structure of p38LZ showed an amphipathic α-helical structure and characteristics similar to a coiled-coil motif. The protein-protein interaction mediated by p38LZ was examined by an in vitro binding assay. The p43 protein, another non-synthetase component of the complex, could bind to p38LZ via its N-terminal domain, which is also predicted to have a potential coiled-coil motif. Thus, we propose that the p38-p43 complex would be formed by coiled-coil interactions, and the formation of the binary complex would facilitate the macromolecular assembly of aminoacyl-tRNA synthetases.

Original languageEnglish
Pages (from-to)119-124
Number of pages6
JournalFEBS Letters
Volume542
Issue number1-3
DOIs
Publication statusPublished - 2003 May 8

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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