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(Received for publication, January 10, 1997, and in revised form, March 26, 1997)
From the Department of Biochemistry and Molecular Biology,
Louisiana State University Medical Center,
Shreveport, Louisiana 71130-3932
To test the hypothesis that
tRNATyr recognition differs between bacterial and
human tyrosyl-tRNA synthetases, we sequenced several clones identified
as human tyrosyl-tRNA synthetase cDNAs by the Human Genome Project.
We found that human tyrosyl-tRNA synthetase is composed of three
domains: 1) an amino-terminal Rossmann fold domain that is responsible
for formation of the activated E·Tyr-AMP intermediate and
is conserved among bacteria, archeae, and eukaryotes; 2) a tRNA
anticodon recognition domain that has not been conserved between
bacteria and eukaryotes; and 3) a carboxyl-terminal domain that is
unique to the human tyrosyl-tRNA synthetase and whose primary structure
is 49% identical to the putative human cytokine endothelial
monocyte-activating protein II, 50% identical to the carboxyl-terminal
domain of methionyl-tRNA synthetase from Caenorhabditis elegans, and 43% identical to the carboxyl-terminal domain of Arc1p from Saccharomyces cerevisiae. The first two domains
of the human tyrosyl-tRNA synthetase are 52, 36, and 16% identical to
tyrosyl-tRNA synthetases from S. cerevisiae,
Methanococcus jannaschii, and Bacillus
stearothermophilus, respectively. Nine of fifteen amino acids
known to be involved in the formation of the tyrosyl-adenylate complex
in B. stearothermophilus are conserved across all of the
organisms, whereas amino acids involved in the recognition of
tRNATyr are not conserved. Kinetic analyses of recombinant
human and B. stearothermophilus tyrosyl-tRNA synthetases
expressed in Escherichia coli indicate that human
tyrosyl-tRNA synthetase aminoacylates human but not B. stearothermophilus tRNATyr, and vice versa,
supporting the original hypothesis. It is proposed that like
endothelial monocyte-activating protein II and the carboxyl-terminal domain of Arc1p, the carboxyl-terminal domain of human tyrosyl-tRNA synthetase evolved from gene duplication of the carboxyl-terminal domain of methionyl-tRNA synthetase and may direct tRNA to the active
site of the enzyme.
Volume 272, Number 22,
Issue of May 30, 1997
pp. 14420-14425
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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