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J. Biol. Chem., Vol. 275, Issue 26, 19913-19920, June 30, 2000
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From the Animal mitochondrial protein synthesis systems
contain two serine tRNAs (tRNAsSer) corresponding to
the codons AGY and UCN, each possessing an unusual secondary structure;
the former lacks the entire D arm, and the latter has a slightly
different cloverleaf structure. To elucidate whether these two
tRNAsSer can be recognized by the single animal
mitochondrial seryl-tRNA synthetase (mt SerRS), we purified mt SerRS
from bovine liver 2400-fold and showed that it can aminoacylate both of
them. Specific interaction between mt SerRS and either of the
tRNAsSer was also observed in a gel retardation assay.
cDNA cloning of bovine mt SerRS revealed that the deduced amino
acid sequence of the enzyme contains 518 amino acid residues. The
cDNAs of human and mouse mt SerRS were obtained by reverse
transcription-polymerase chain reaction and expressed sequence tag data
base searches. Elaborate inspection of primary sequences of mammalian
mt SerRSs revealed diversity in the N-terminal domain responsible for
tRNA recognition, indicating that the recognition mechanism of
mammalian mt SerRS differs considerably from that of its prokaryotic
counterpart. In addition, the human mt SerRS gene was found to be
located on chromosome 19q13.1, to which the autosomal deafness locus
DFNA4 is mapped.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AB029947 (bovine mt SerRS), AB029948 (human mt SerRS), and AB029949 (mouse mt SerRS).
Characterization and tRNA Recognition of Mammalian Mitochondrial
Seryl-tRNA Synthetase*
§,
,,,,¶¶
Department of Biomolecular Science, Faculty
of Engineering, Gifu University, 1-1 Yanagito, Gifu 501-1193, Japan,
the ¶ Department of Chemistry and Biotechnology, Graduate School
of Engineering, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo
113-8656, Japan, the Laboratoire de Biochimie, École de
Polytechnique, Palaiseau, F-91128, France, the ** Department of
Chemistry, University of North Carolina, Chapel Hill, North Carolina
27599-3290, the Department of Integrated
Biosciences, Graduate School of Frontier Sciences, University of Tokyo
113-8656, Japan, and the §§ Mitsubishi-Kasei
Institute of Life Sciences, 11 Minamiooya, Machida-shi,
Tokyo 194, Japan
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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