Genome Research

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Aravind, L.
Right arrow Articles by Koonin, E. V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Aravind, L.
Right arrow Articles by Koonin, E. V.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Vol. 10, Issue 8, 1172-1184, August 2000

LETTER
Eukaryote-specific Domains in Translation Initiation Factors: Implications for Translation Regulation and Evolution of the Translation System

L. Aravind,1 and Eugene V. Koonin

1 National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20894 USA

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.

1 Corresponding author.

10:1172-1184 ©2000 by Cold Spring Harbor Laboratory Press  ISSN 1088-9051/00 $5.00
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
C. Suzuki, R. G. Garces, K. A. Edmonds, S. Hiller, S. G. Hyberts, A. Marintchev, and G. Wagner
PDCD4 inhibits translation initiation by binding to eIF4A using both its MA3 domains
PNAS, March 4, 2008; 105(9): 3274 - 3279.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. Hedges, Y.-I Chen, M. West, C. Bussiere, and A. W. Johnson
Mapping the Functional Domains of Yeast NMD3, the Nuclear Export Adapter for the 60 S Ribosomal Subunit
J. Biol. Chem., December 1, 2006; 281(48): 36579 - 36587.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. V. Alone and T. E. Dever
Direct Binding of Translation Initiation Factor eIF2{gamma}-G Domain to Its GTPase-activating and GDP-GTP Exchange Factors eIF5 and eIF2B{epsilon}
J. Biol. Chem., May 5, 2006; 281(18): 12636 - 12644.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
C. R. Singh, C. Curtis, Y. Yamamoto, N. S. Hall, D. S. Kruse, H. He, E. M. Hannig, and K. Asano
Eukaryotic Translation Initiation Factor 5 Is Critical for Integrity of the Scanning Preinitiation Complex and Accurate Control of GCN4 Translation
Mol. Cell. Biol., July 1, 2005; 25(13): 5480 - 5491.
[Abstract] [Full Text] [PDF]

Home page
 RNAHome page
H. ZAKOWICZ, H.-S. YANG, C. STARK, A. WLODAWER, N. LARONDE-LEBLANC, and N. H. COLBURN
Mutational analysis of the DEAD-box RNA helicase eIF4AII characterizes its interaction with transformation suppressor Pdcd4 and eIF4GI
RNA, March 1, 2005; 11(3): 261 - 274.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. R. Singh, Y. Yamamoto, and K. Asano
Physical Association of Eukaryotic Initiation Factor (eIF) 5 Carboxyl-terminal Domain with the Lysine-rich eIF2{beta} Segment Strongly Enhances Its Binding to eIF3
J. Biol. Chem., November 26, 2004; 279(48): 49644 - 49655.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
H.-S. Yang, M.-H. Cho, H. Zakowicz, G. Hegamyer, N. Sonenberg, and N. H. Colburn
A Novel Function of the MA-3 Domains in Transformation and Translation Suppressor Pdcd4 Is Essential for Its Binding to Eukaryotic Translation Initiation Factor 4A
Mol. Cell. Biol., May 1, 2004; 24(9): 3894 - 3906.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
S.-Y. Chiu, F. Lejeune, A. C. Ranganathan, and L. E. Maquat
The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex
Genes & Dev., April 1, 2004; 18(7): 745 - 754.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
A. Nott, H. Le Hir, and M. J. Moore
Splicing enhances translation in mammalian cells: an additional function of the exon junction complex
Genes & Dev., January 15, 2004; 18(2): 210 - 222.
[Abstract] [Full Text] [PDF]

Home page
 RNAHome page
J. BARON-BENHAMOU, P. FORTES, T. INADA, T. PREISS, and M. W. HENTZE
The interaction of the cap-binding complex (CBC) with eIF4G is dispensable for translation in yeast
RNA, June 1, 2003; 9(6): 654 - 662.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
H.-S. Yang, A. P. Jansen, A. A. Komar, X. Zheng, W. C. Merrick, S. Costes, S. J. Lockett, N. Sonenberg, and N. H. Colburn
The Transformation Suppressor Pdcd4 Is a Novel Eukaryotic Translation Initiation Factor 4A Binding Protein That Inhibits Translation
Mol. Cell. Biol., January 1, 2003; 23(1): 26 - 37.
[Abstract] [Full Text]

Home page
 Genome Res.Home page
O. Lespinet, Y. I. Wolf, E. V. Koonin, and L. Aravind
The Role of Lineage-Specific Gene Family Expansion in the Evolution of Eukaryotes
Genome Res., July 1, 2002; 12(7): 1048 - 1059.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
V. Anantharaman, E. V. Koonin, and L. Aravind
Comparative genomics and evolution of proteins involved in RNA metabolism
Nucleic Acids Res., April 1, 2002; 30(7): 1427 - 1464.
[Abstract] [Full Text] [PDF]

Home page
 Genome Res.Home page
E. V. Koonin, Y. I. Wolf, and L. Aravind
Prediction of the Archaeal Exosome and Its Connections with the Proteasome and the Translation and Transcription Machineries by a Comparative-Genomic Approach
Genome Res., February 1, 2001; 11(2): 240 - 252.
[Abstract] [Full Text]

Home page
 Mol. Cell. Biol.Home page
G. Serin, A. Gersappe, J. D. Black, R. Aronoff, and L. E. Maquat
Identification and Characterization of Human Orthologues to Saccharomyces cerevisiae Upf2 Protein and Upf3 Protein (Caenorhabditis elegans SMG-4)
Mol. Cell. Biol., January 1, 2001; 21(1): 209 - 223.
[Abstract] [Full Text]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Genes Dev. Learn. Mem.
Protein Science RNA Genome Res.