Highly homologous eEF1A1 and eEF1A2 exhibit differential post-translational modification with significant enrichment around localised sites of sequence variation.
This article was reviewed by Frank Eisenhaber and Ramanathan Sowdhamini.Translation elongation factors eEF1A1 and eEF1A2 are 92% identical but exhibit non-overlapping expression patterns. While the two proteins are predicted to have similar tertiary structures, it is notable that the minor variations between their sequences are highly localised within their modelled structures. We used recently available high-throughput "omics" data to assess the spatial location of post-translational modifications and discovered that they are highly enriched on those surface regions of the protein that correspond to the clusters of sequence variation. This observation suggests how these two isoforms could be differentially regulated allowing them to perform distinct functions.
Dinesh C
DC
Soares
Catherine M
CM
Abbott
D014644:Genetic Variation; D020648:Peptide Elongation Factor 1 / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D017422:Sequence Analysis, DNA
C094814:EEF1A1 protein, human; C503234:EEF1A2 protein, human; D020648:Peptide Elongation Factor 1; D020033:Protein Isoforms