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Journal of Biochemistry Advance Access published online on May 26, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp078
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Domain-dependent interaction of eukaryotic initiation factor eIF4A for binding to middle and C-terminal domains of eIF4G

Yuki Fujita1, Masako Oe1, Tatsuya Tutsumino1, Shigenobu Morino1,*, Hiroaki Imataka2, Koji Tomoo1,{dagger} and Toshimasa Ishida1

1 Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-1094, Japan; and 2 Riken Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama City, Kanagawa, 230-0045, Japan

* Present address: Screening Science, Lead Discovery Research Labs. Drug Discovery Research Astellas Pharma Inc. 21, Miyukigaoka, Tsukuba-shi, Ibaraki 305-8585, Japan

Received April 28, 2009; Accepted May 11, 2009


  Abstract

The interactions of recombinant human eIF4A (4A) and its N- and C-terminal side domains (AN and AC, respectively) with the middle- and C-terminal-domain-linked fragment (GMC) of eIF4G and its middle and C-terminal domains (GM and GC, respectively) were investigated by surface plasmon resonance (SPR) analysis and isothermal titration calorimetry (ITC). It is remarkable that the kinetic parameter-dependent SPR profile observed for the 4A-GMC pair was quite different from the steady affinity profiles of the 4A-GM/GC pairs, suggesting the simultaneous contribution of the middle and C-terminal domains of eIF4G for the binding with eIF4A. On the other hand, ITC yielded the enthalpy energies of -1.5 ~ -2.5 x104 J/mol for the domain-domain interactions of 4A with GMC. Although the ITC profile of the 4A-GM pair reflects well the structural feature shown previously by NMR and X-ray analyses, it was essentially different from that of the 4A-GMC pair. The present results suggest that the intimate interaction between the eIF4A N- and C-terminal domains and the eIF4G middle and C-terminal domains is necessary to reveal the biologically active function of the eIF4A-eIF4G complex.

Key Words: eIF4A, eIF4G, association, domain-domain interaction, surface plasmon resonance, isothermal titration calorimetry

{dagger}To whom correspondence should be addressed: Dr. Tomoo, Koji, Tel: +81-72-690-1069, Fax: +81-72-690-1068 E-mail: tomoo{at}gly.oups.ac.jp


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