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Science 24 January 1997:
Vol. 275. no. 5299, pp. 500 - 501
DOI: 10.1126/science.275.5299.500
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Perspectives

Matthias W. Hentze

Messenger RNAs are translated into protein--a complex enterprise. Now, in work from a number of laboratories, one small adapter protein is shown to be a central player in several variations on the process. In his Perspective, Hentze describes how eIF4G serves as an adapter that binds the small ribosome subunit to the messenger RNA, working in different ways when the message has a 7mG cap at its 5' end or a polyadenylated tail at its 3' end.

The author is at the Gene Expression Programme, European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany. E-mail: matthias.hentze{at}EMBL-Heidelberg.de

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Translational Repression by Human 4E-BP1 in Yeast Specifically Requires Human eIF4E as Target.
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Posttranscriptional Control of Gene Expression in Yeast.
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Rapamycin and Wortmannin Enhance Replication of a Defective Encephalomyocarditis Virus.
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X. Wang, A. Flynn, A. J. Waskiewicz, B. L. J. Webb, R. G. Vries, I. A. Baines, J. A. Cooper, and C. G. Proud (1998)
J. Biol. Chem. 273, 9373-9377
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The TOR (target of rapamycin) signal transduction pathway regulates the stability of translation initiation factor eIF4G in the yeast Saccharomyces cerevisiae.
C. Berset, H. Trachsel, and M. Altmann (1998)
PNAS 95, 4264-4269
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A Novel Functional Human Eukaryotic Translation Initiation Factor 4G.
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Mol. Cell. Biol. 18, 334-342
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In vitro selection of a 7-methyl-guanosine binding RNA that inhibits translation of capped mRNA molecules.
A. A. Haller and P. Sarnow (1997)
PNAS 94, 8521-8526
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HIV-1 protease cleaves eukaryotic initiation factor 4G and inhibits cap-dependent translation.
I. Ventoso, R. Blanco, C. Perales, and L. Carrasco (2001)
PNAS 98, 12966-12971
   Abstract »    Full Text »    PDF »


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