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Folding transitions during assembly of the eukaryotic mRNA cap-binding complex.

Abstract：

:The cap-binding protein eIF4E is the first in a chain of translation initiation factors that recruit 40S ribosomal subunits to the 5' end of eukaryotic mRNA. During cap-dependent translation, this protein binds to the 5'-terminal m(7)Gppp cap of the mRNA, as well as to the adaptor protein eIF4G. The latter then interacts with small ribosomal subunit-bound proteins, thereby promoting the mRNA recruitment process. Here, we show apo-eIF4E to be a protein that contains extensive unstructured regions, which are induced to fold upon recognition of the cap structure. Binding of eIF4G to apo-eIF4E likewise induces folding of the protein into a state that is similar to, but not identical with, that of cap-bound eIF4E. At the same time, binding of each of the binding partners of eIF4E modulates the kinetics with which it interacts with the other partner. We present structural, kinetic and mutagenesis data that allow us to deduce some of the detailed folding transitions that take place during the eIF4E interactions.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

von der Haar T,Oku Y,Ptushkina M,Moerke N,Wagner G,Gross JD,McCarthy JE

doi

10.1016/j.jmb.2005.12.034

keywords:

subject

Has Abstract

pub_date

2006-03-03 00:00:00

pages

982-92

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(05)01596-2

journal_volume

356

pub_type

杂志文章

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