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PMID: 10958635 Published · ppublish English Journal Article

Eukaryote-specific domains in translation initiation factors: implications for translation regulation and evolution of the translation system.

Genome research ·Vol. 10 ·No. 8 ·2000-08-00 ·Pages 1172-84

Aravind L, Koonin EV

Abstract

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 alpha-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 alpha-helical domain is delineated in the initiation factor eIF4G, in Nonsense-mediated mRNA decay 2 protein (NMD2/UPF2), in the nuclear cap-binding CBP80, and in other, poorly characterized proteins, which is named the NIC (NMD2, eIF4G, CBP80) 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 (MA-3 and eIF4G ) and W2, which probably was accompanied by acquisition of new regulatory interactions.

MeSH Terms
Adaptor Proteins, Signal Transducing Amino Acid Sequence Animals Conserved Sequence Databases, Factual Eukaryotic Cells/chemistry,physiology Evolution, Molecular Fungal Proteins/chemistry,genetics Humans Molecular Sequence Data Peptide Initiation Factors/chemistry,genetics Phylogeny Protein Biosynthesis Protein Structure, Tertiary Saccharomyces cerevisiae Proteins Trans-Activators/chemistry,genetics
Chemicals
Adaptor Proteins, Signal Transducing Fungal Proteins NMD2 protein, S cerevisiae Peptide Initiation Factors Saccharomyces cerevisiae Proteins Trans-Activators eIF-4gamma
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Aravind L
National Center for Biotechnology Information, National Library of Medicine, National Institute of Health, Bethesda, MD 20894, USA. aravind@ncbi.nlm.nih.gov
Koonin E V
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Article Info
Journal
Genome research
Abbr.
Genome Res
ISSN
1088-9051
DOI
10.1101/gr.10.8.1172
Email
aravind@ncbi.nlm.nih.gov
Published
2000-08-00
Pages
1172-84
Language
English
Region
United States
NLM ID
9518021
PMCID
PMC310937
Subset
IM
External Links
PubMed source DOI: 10.1101/gr.10.8.1172 PMC Full Text View journal details
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