期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 284, 期 21, 页码 14096-14104出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M808173200
关键词
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资金
- Agence Nationale de la Recherche, 2005-2008
Several L-aminoacyl-tRNA synthetases can transfer a D-amino acid onto their cognate tRNA(s). This harmful reaction is counteracted by the enzyme D-aminoacyl-tRNA deacylase. Two distinct deacylases were already identified in bacteria (DTD1) and in archaea (DTD2), respectively. Evidence was given that DTD1 homologs also exist in nearly all eukaryotes, whereas DTD2 homologs occur in plants. On the other hand, several bacteria, including most cyanobacteria, lack genes encoding a DTD1 homolog. Here we show that Synechocystis sp. PCC6803 produces a third type of deacylase (DTD3). Inactivation of the corresponding gene (dtd3) renders the growth of Synechocystis sp. hypersensitive to the presence of D-tyrosine. Based on the available genomes, DTD3-like proteins are predicted to occur in all cyanobacteria. Moreover, one or several dtd3-like genes can be recognized in all cellular types, arguing in favor of the near-ubiquity of an enzymatic function involved in the defense of translational systems against invasion by D-amino acids.
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