Crystal structures of ribosome anti-association factor IF6
Ribosome anti-association factor eIF6 (originally named according to translation initiation terminology as eukaryotic initiation factor 6) binds to the large ribosomal subunit, thereby preventing inappropriate interactions with the small subunit during initiation of protein synthesis. We have determ...
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Veröffentlicht in: | Nature Structural Biology 2000-12, Vol.7 (12), p.1156-1164 |
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Sprache: | eng |
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Zusammenfassung: | Ribosome anti-association factor eIF6 (originally named according to translation initiation terminology as eukaryotic initiation factor 6) binds to the large ribosomal subunit, thereby preventing inappropriate interactions with the small subunit during initiation of protein synthesis. We have determined the X-ray structures of two IF6 homologs,
Methanococcus jannaschii
archaeal aIF6 and
Sacchromyces cerevisiae
eIF6, revealing a phylogenetically conserved 25 kDa protein consisting of five quasi identical α/β subdomains arrayed about a five-fold axis of pseudosymmetry. Yeast eIF6 prevents ribosomal subunit association. Comparative protein structure modeling with other known archaeal and eukaryotic homologs demonstrated the presence of two conserved surface regions, one or both of which may bind the large ribosomal subunit. |
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ISSN: | 1072-8368 1545-9993 1545-9985 |
DOI: | 10.1038/82017 |