Eukaryote-specific Domains in Translation Initiation Factors: Implications for Translation Regulation and Evolution of the Translation System
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Computational analysis of sequences of proteins involved in translation initiation in eukaryotes reveals a number of specific domains that are not represented in bacteria or archaea. Most of these eukaryote-specific domains are known or predicted to possess an α-helical structure, which suggests that such domains are easier to invent in the course of evolution than are domains of other structural classes. A previously undetected, conserved region predicted to form an α-helical domain is delineated in the initiation factor eIF4G, in N onsense-mediated m RNA d ecay 2 protein (NMD2/UPF2), in the nuclear cap-binding CBP80, and in other, poorly characterized proteins, which is named the NIC (N MD2, e I F4G, C BP80) domain. Biochemical and mutagenesis data on NIC-containing proteins indicate that this predicted domain is one of the central adapters in the regulation of mRNA processing, translation, and degradation. It is demonstrated that, in the course of eukaryotic evolution, initiation factor eIF4G, of which NIC is the core, conserved portion, has accreted several additional, distinct predicted domains such as MI (M A-3 and e I F4G ) and W2, which probably was accompanied by acquisition of new regulatory interactions.
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PDCD4 protein contains two MA3 domains homologous to the M1 domain of eIF4G.
“PDCD4-protein contains two MA3 domains homologous to the M1 domain of eukaryotic translation initiation factor 4G (eIF4G) [23] (Figure 2).”
From Control Mechanisms of the Tumor Suppressor PDCD4: Expression and Functions (2019) · cites this paper as [23]
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Characterization of the mIF4G domains in the RNA surveillance protein Upf2Preprint
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Evolution of histone mRNA 3’ end processing machinery in eukaryotesPreprint
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- Authors
- Aravind, L., & Koonin, E. V.
- Affiliations
- National Institutes of Health (US)
- Venue
- Genome Research
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2000-08-01
- Volume
- 10
- Issue
- 8
- Pages
- 1172-1184
- ISSN
- 1088-9051 (ISSN-L)
- 1549-5469
- PMC
- PMC310937
- OpenAlex
- W2085625054
- Cited by
- 93
- References
- 62
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 1 · 2023: 3 · 2022: 7 · 2021: 2 · 2020: 1 · 2019: 1 · 2018: 6 · 2017: 2 · 2016: 3 · 2015: 3 · 2014: 6 · 2013: 4 · 2012: 5
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genome Research (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- eukaryotic translation initiation factors, eIF4G, CBP80, nonsense-mediated mRNA decay, alpha-helical domain, domain evolution, translational regulation, mRNA processing, eukaryotic evolution
- MeSH terms
- Amino Acid Sequence, Animals, Eukaryotic Cells, Fungal Proteins, Humans, Molecular Sequence Data, Peptide Initiation Factors, Phylogeny, Protein Biosynthesis, Trans-Activators, Databases, Factual, Conserved Sequence, Protein Structure, Tertiary, Evolution, Molecular, Saccharomyces cerevisiae Proteins, Adaptor Proteins, Signal Transducing
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