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Protein Science, Vol 3, Issue 11 2045-2054, Copyright © 1994 by Cold Spring Harbor Laboratory Press

ARTICLE

Eukaryotic translation elongation factor 1{gamma} contains a glutathione transferase domain--Study of a diverse, ancient protein superfamily using motif search and structural modeling

E. V. KOONIN, A. R. MUSHEGIAN, R. L. TATUSOV, S. F. ALTSCHUL, S. H. BRYANT, P. BORK and A. VALENCIA
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20894

Using computer methods for multiple alignment, sequence motif search, and tertiary structure modeling, we show that eukaryotic translation elongation factor 1{gamma} (EF1{gamma}) contains an N-terminal domain related to class {theta} glutathione S-transferases (GST). GST-like proteins related to class {theta} comprise a large group including, in addition to typical GSTs and EF1{gamma}, stress-induced proteins from bacteria and plants, bacterial reductive dehalogenases and {beta}-etherases, and several uncharacterized proteins. These proteins share 2 conserved sequence motifs with GSTs of other classes ({alpha}, {mu}, and {pi}). Tertiary structure modeling showed that in spite of the relatively low sequence similarity, the GST-related domain of EF1{gamma} is likely to form a fold very similar to that in the known structures of class {alpha}, {mu}, and {pi} GSTs. One of the conserved motifs is implicated in glutathione binding, whereas the other motif probably is involved in maintaining the proper conformation of the GST domain. We predict that the GST-like domain in EF1{gamma} is enzymatically active and that to exhibit GST activity, EF1{gamma} has to form homodimers. The GST activity may be involved in the regulation of the assembly of multisubunit complexes containing EF1 and aminoacyl-tRNA synthetases by shifting the balance between glutathione, disulfide glutathione, thiol groups of cysteines, and protein disulfide bonds. The GST domain is a widespread, conserved enzymatic module that may be covalently or noncovalently complexed with other proteins. Regulation of protein assembly and folding may be 1 of the functions of GST.
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Copyright © 1994 by The Protein Society.