HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Fechter, P. Articles by Brownlee, G. G. Search for Related Content PubMed PubMed Citation Articles by Fechter, P. Articles by Brownlee, G. G. Agricola Articles by Fechter, P. Articles by Brownlee, G. G.

Recognition of mRNA cap structures by viral and cellular proteins

Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK

Correspondence
George G. Brownlee
George.Brownlee{at}path.ox.ac.uk

Most cellular and eukaryotic viral mRNAs have a cap structure at their 5' end that is critical for efficient translation. Cap structures also aid in mRNA transport from nucleus to cytoplasm and, in addition, protect the mRNAs from degradation by 5' exonucleases. Cap function is mediated by cap-binding proteins that play a key role in translational control. Recent structural studies on the cellular cap-binding complex, the eukaryotic translation initiation factor 4E and the vaccinia virus protein 39, suggest that these three evolutionary unrelated cap-binding proteins have evolved a common cap-binding pocket by convergent evolution. In this pocket the positively charged N⁷-methylated guanine ring of the cap structure is stacked between two aromatic amino acids. In this review, the similarities and differences in cap binding by these three different cap-binding proteins are discussed. A comparison with new functional data for another viral cap-binding protein – the polymerase basic protein (PB2) of influenza virus – suggests that a similar cap-binding mechanism has also evolved in influenza virus.

Published online ahead of print on 10 February 2005 as DOI 10.1099/vir.0.80755-0.

This article has been cited by other articles:

				R. Assenberg, J. Ren, A. Verma, T. S. Walter, D. Alderton, R. J. Hurrelbrink, S. D. Fuller, S. Bressanelli, R. J. Owens, D. I. Stuart, et al. Crystal structure of the Murray Valley encephalitis virus NS5 methyltransferase domain in complex with cap analogues J. Gen. Virol., August 1, 2007; 88(8): 2228 - 2236. [Abstract] [Full Text] [PDF]

				J. Zuberek, D. Kubacka, A. Jablonowska, J. Jemielity, J. Stepinski, N. Sonenberg, and E. Darzynkiewicz Weak binding affinity of human 4EHP for mRNA cap analogs RNA, May 1, 2007; 13(5): 691 - 697. [Abstract] [Full Text] [PDF]

				J. R. Zamudio, B. Mittra, G. M. Zeiner, M. Feder, J. M. Bujnicki, N. R. Sturm, and D. A. Campbell Complete Cap 4 Formation Is Not Required for Viability in Trypanosoma brucei Eukaryot. Cell, June 1, 2006; 5(6): 905 - 915. [Abstract] [Full Text] [PDF]

				S. V. Slepenkov, E. Darzynkiewicz, and R. E. Rhoads Stopped-flow Kinetic Analysis of eIF4E and Phosphorylated eIF4E Binding to Cap Analogs and Capped Oligoribonucleotides: EVIDENCE FOR A ONE-STEP BINDING MECHANISM J. Biol. Chem., May 26, 2006; 281(21): 14927 - 14938. [Abstract] [Full Text] [PDF]

				J. K. Ospina, G. B. Gonsalvez, J. Bednenko, E. Darzynkiewicz, L. Gerace, and A. G. Matera Cross-Talk between Snurportin1 Subdomains Mol. Biol. Cell, October 1, 2005; 16(10): 4660 - 4671. [Abstract] [Full Text] [PDF]

				M. J. Moore From Birth to Death: The Complex Lives of Eukaryotic mRNAs Science, September 2, 2005; 309(5740): 1514 - 1518. [Abstract] [Full Text] [PDF]