Maize seryl-tRNA synthetase: Specificity of substrate recognition by the organellar enzyme

被引:13
|
作者
Rokov-Plavec, J
Lesjak, S
Landeka, I
Mijakovic, I
Weygand-Durasevic, I
机构
[1] Univ Zagreb, Fac Sci, Dept Chem, Zagreb 10000, Croatia
[2] Rudjer Boskovic Inst, Zagreb 10000, Croatia
基金
美国国家卫生研究院;
关键词
seryl-tRNA synthetases; organelles; Zea mays; tRNA-dependent amino acid recognition; complementation;
D O I
10.1006/abbi.2001.2600
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In our study of seryl-tRNA formation in maize, we investigated the enzymes involved in serylation. Only two dissimilar seryl-tRNA synthetase (SerRS) cDNA clones were identified in the Zea mays EST (expressed sequence tag) databases. One encodes a seryl-tRNA synthetase, which presumably functions in the organelles (SerZMm), while the other synthetase product is more similar to eukaryotic cytosolic counterparts (SerZMc). The expression of SerZMm in Saccharomyces cerevisiae resulted in complementation of mutant respiratory phenotype, caused by a disruption of the nuclear gene, presumably encoding yeast mitochondrial seryl-tRNA synthetase (SerSCm). Purified mature SerZMm displays tRNA-assisted serine activation and aminoacylates maize mitochondrial and chloroplast tRNA(Ser) transcripts with similar efficiencies, raising the possibility that only two isoforms of seryl-tRNA synthetase may be sufficient to catalyze seryl-tRNA(Ser) formation in three cellular compartments of Zea mays. Phylogenetic analysis suggests that SerZMm is of mitochondrial origin. (C) 2001 Elsevier Science.
引用
收藏
页码:40 / 50
页数:11
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