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Journal of Bacteriology, December 2008, p. 7876-7884, Vol. 190, No. 24
0021-9193/08/$08.00+0 doi:10.1128/JB.00874-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Department of Microbiology and Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611,1 Donald Danforth Plant Science Center, St. Louis, Missouri 63132,2 Department of Chemistry, Portland State University, Portland, Oregon 972073
Received 25 June 2008/ Accepted 7 October 2008
Queuosine (Q) and archaeosine (G+) are hypermodified ribonucleosides found in tRNA. Q is present in the anticodon region of tRNAGUN in Eukarya and Bacteria, while G+ is found at position 15 in the D-loop of archaeal tRNA. Prokaryotes produce these 7-deazaguanosine derivatives de novo from GTP through the 7-cyano-7-deazaguanine (pre-Q0) intermediate, but mammals import the free base, queuine, obtained from the diet or the intestinal flora. By combining the results of comparative genomic analysis with those of genetic studies, we show that the first enzyme of the folate pathway, GTP cyclohydrolase I (GCYH-I), encoded in Escherichia coli by folE, is also the first enzyme of pre-Q0 biosynthesis in both prokaryotic kingdoms. Indeed, tRNA extracted from an E. coli
folE strain is devoid of Q and the deficiency is complemented by expressing GCYH-I-encoding genes from different bacterial or archaeal origins. In a similar fashion, tRNA extracted from a Haloferax volcanii strain carrying a deletion of the GCYH-I-encoding gene contains only traces of G+. These results link the production of a tRNA-modified base to primary metabolism and further clarify the biosynthetic pathway for these complex modified nucleosides.
Published ahead of print on 17 October 2008.
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