A lysine substitution in the ATP-binding site of eucaryotic initiation factor 4A abrogates nucleotide-binding activity.

Abstract:

:Eucaryotic initiation factor 4A (eIF-4A) is a member of a family of proteins believed to be involved in the ATP-dependent melting of RNA secondary structure. These proteins contain a derivative of the consensus ATP-binding site AXXGXGKT. To assess the importance of the consensus amino acid sequence in eIF-4A for ATP binding, we mutated the consensus amino-proximal glycine and lysine to isoleucine and asparagine, respectively. The effect of the mutations was examined by UV-induced cross-linking of [alpha-32P]dATP to eIF-4A. Mutation of the lysine residue (but not of the glycine residue) resulted in the loss of [alpha-32P]dATP cross-linking to eIF-4A, suggesting that the lysine is an important determinant in ATP binding to eIF-4A.

journal_name

Mol Cell Biol

authors

Rozen F,Pelletier J,Trachsel H,Sonenberg N

doi

10.1128/mcb.9.9.4061

subject

Has Abstract

pub_date

1989-09-01 00:00:00

pages

4061-3

issue

9

eissn

0270-7306

issn

1098-5549

journal_volume

9

pub_type

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