Biochemical Selenosysteine Synthesis and the Phylogenic Study
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- MIZUTANI Takaharu
- Graduate School of Pharmaceutical Sciences, Nagoya City University
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- OSAKA Takashi
- Graduate School of Pharmaceutical Sciences, Nagoya City University
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- FUJIWARA Toshinobu
- Graduate School of Engineering, Kobe University
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- Shahidzzman M.
- Graduate School of Pharmaceutical Sciences, Nagoya City University
Bibliographic Information
- Other Title
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- セレノシステイン生合成系とその種多様性
- セレノシステイン セイゴウセイケイ ト ソノ シュ タヨウセイ
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Abstract
Selenium (Se) is an essential trace element. Se is found as selenocysteine (Sec) in Se-proteins. Sec is the 21st amino acid, because Sec has its tRNA, the codon UGA and those components in its translational machinery. Sec UGA codon shares with major stop codon UGA. We purified Sec synthesizing enzymes, such as seryl-tRNA synthetase (SerRS), Sec synthetase (SecS) and selenophosphate synthetase (SePS). I described the procedures to prepare Sec tRNA, SerRS, SecS, SePS and [75Se]H2Se in detail. We clarified that SecS composed of two proteins, SecSα and SecSβ. Sec synthesizing and incorporating systems present in Monela, Animalia and Protoctista but not in Plantae and Fungi. We showed that protozoa had Sec tRNA on which Sec was synthesized from Ser-tRNA by bovine and protozoa SecS. Some worms, such as Caenorhabditis elegans and Fasiola gigantica, also had Sec tRNA on which Sec was synthesized by bovine liver SecS or C. elegans enzymes. We showed recognition sites of mammalian Sec tRNA by SecS. The identitiy units of Sec tRNA are 9 bp aminoacyl- and 6 bp D-stems. This recognition is not the base-specific manner but the length-specific manner. From comparison of the phylogeny trees of Sec synthesizing system and translation system, we concluded that the evolution of Sec synthesizing system is older than that of the translation system.<br>
Journal
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- YAKUGAKU ZASSHI
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YAKUGAKU ZASSHI 128 (7), 989-996, 2008-07-01
The Pharmaceutical Society of Japan
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Details 詳細情報について
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- CRID
- 1390282681106007552
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- NII Article ID
- 110006792628
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- NII Book ID
- AN00284903
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- ISSN
- 13475231
- 00316903
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- NDL BIB ID
- 9571803
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed