TY - JOUR
T1 - Solution structure and p43 binding of the p38 leucine zipper motif
T2 - Coiled-coil interactions mediate the association between p38 and p43
AU - Ahn, Hee Chul
AU - Kim, Sunghoon
AU - Lee, Bong Jin
PY - 2003/5/8
Y1 - 2003/5/8
N2 - 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.
AB - 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.
KW - Coiled-coil motif
KW - Macromolecular tRNA synthetase complex
KW - Nuclear magnetic resonance
KW - Protein-protein interaction
UR - http://www.scopus.com/inward/record.url?scp=0038405007&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(03)00362-4
DO - 10.1016/S0014-5793(03)00362-4
M3 - Article
C2 - 12729910
AN - SCOPUS:0038405007
SN - 0014-5793
VL - 542
SP - 119
EP - 124
JO - FEBS Letters
JF - FEBS Letters
IS - 1-3
ER -