ArticleNucleic acids research2003
Assessing functional divergence in EF-1alpha and its paralogs in eukaryotes and archaebacteria.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 34 citations in OpenAlex.
- Nucleomorph phylogenomics suggests a deep and ancient origin of cryptophyte plastids within Rhodophyta.The New phytologist · 2026Article
- A ribosome-associating chaperone mediates GTP-driven vectorial folding of nascent eEF1A.Nature communications · 2025Article
- In Silico Structural Modeling and Analysis of Elongation Factor-1 Alpha and Elongation Factor-like Protein.ACS omega · 2019Article
- The Origin and Evolution of Release Factors: Implications for Translation Termination, Ribosome Rescue, and Quality Control Pathways.International journal of molecular sciences · 2019Review
- ABCE Proteins: From Molecules to Development.Frontiers in plant science · 2018Review
- Recent structural studies on Dom34/aPelota and Hbs1/aEF1α: important factors for solving general problems of ribosomal stall in translation.Biophysics (Nagoya-shi, Japan) · 2013Review
- Influence of histatin 5 on Candida albicans mitochondrial protein expression assessed by quantitative mass spectrometry.Journal of proteome research · 2011Article
- Dissection of Dom34-Hbs1 reveals independent functions in two RNA quality control pathways.Nature structural & molecular biology · 2010Article
- Structural basis for mRNA surveillance by archaeal Pelota and GTP-bound EF1α complex.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- GTP-dependent structural rearrangement of the eRF1:eRF3 complex and eRF3 sequence motifs essential for PABP binding.Nucleic acids research · 2010Article
- Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components.BMC evolutionary biology · 2008Article
- A mixed branch length model of heterotachy improves phylogenetic accuracy.Molecular biology and evolution · 2008Article
- Article
- A class of eukaryotic GTPase with a punctate distribution suggesting multiple functional replacements of translation elongation factor 1alpha.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Evolution of eukaryotic transcription: insights from the genome of Giardia lamblia.Genome research · 2004Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
A number of methods have recently been published that use phylogenetic information extracted from large multiple sequence alignments to detect sites that have changed properties in related protein families. In this study we use such methods to assess functional divergence between eukaryotic EF-1alpha (eEF-1alpha), archaebacterial EF-1alpha (aEF-1alpha) and two eukaryote-specific EF-1alpha paralogs-eukaryotic release factor 3 (eRF3) and Hsp70 subfamily B suppressor 1 (HBS1). Overall, the evolutionary modes of aEF-1alpha, HBS1 and eRF3 appear to significantly differ from that of eEF-1alpha. However, functionally divergent (FD) sites detected between aEF-1alpha and eEF-1alpha only weakly overlap with sites implicated as putative EF-1beta or aminoacyl-tRNA (aa-tRNA) binding residues in EF-1alpha, as expected based on the shared ancestral primary translational functions of these two orthologs. In contrast, FD sites detected between eEF-1alpha and its paralogs significantly overlap with the putative EF-1beta and/or aa-tRNA binding sites in EF-1alpha. In eRF3 and HBS1, these sites appear to be released from functional constraints, indicating that they bind neither eEF-1beta nor aa-tRNA. These results are consistent with experimental observations that eRF3 does not bind to aa-tRNA, but do not support the 'EF-1alpha-like' function recently proposed for HBS1. We re-assess the available genetic data for HBS1 in light of our analyses, and propose that this protein may function in stop codon-independent peptide release.
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