Characterization of Human Selenocysteine Synthase Involved in Selenoprotein Biosynthesis

• Abe Katsumasa

  Institute for Chemical Research, Kyoto University

• Mihara Hisaaki

  Institute for Chemical Research, Kyoto University

• Tobe Ryuta

  Institute for Chemical Research, Kyoto University

• Esaki Nobuyoshi

  Institute for Chemical Research, Kyoto University

抄録

Bacterial selenocysteine synthase is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes the conversion of seryl-tRNA^Sec to selenocysteyl-tRNA^Sec for selenoprotein biosynthesis. Human selenocysteine synthase(SecS),originally annotated as SLA/LP, was previously reported to operate in selenocysteyl-tRNA^Sec synthesis, but the mechanism of conversion from Ser-tRNA^Sec by the eukaryotic enzyme remained unresolved. Herein, the human cDNA encoding SecS has been cloned and overexpressed in Escherichia coli. SecS was co-purified with E. coli tRNAs, which was revealed to contain tRNA^Sec by PCR analysis. The purified enzyme exhibited a UV-visible absorption maximum at 420 nm characteristic of pyridoxal 5'-phosphate-dependent enzymes. In vitro selenocysteyl-tRNA^Sec synthesis assay suggests that the formation of phosphoseryl-tRNA^Sec is essential for human seryl-tRNA^Sec, but not archaeal seryl-tRNA^Sec to be converted to selenocysteyl-tRNA^Sec by human SecS.

収録刊行物

• Biomedical Research on Trace Elements

  Biomedical Research on Trace Elements 19 (1), 80-83, 2008

  日本微量元素学会

キーワード

• selenoprotein
• selenocysteine synthase
• selenium
• human
• biosynthesis

詳細情報

• CRID: 1390282679344511744
• NII論文ID: 130004456855
• NII論文ID: 10021098073
• NII書誌ID: AN10423256
• DOI: 10.11299/brte.19.80
• ISSN: 18801404
• ISSN: 0916717X
• NDL書誌ID: 9542150
• Web Site: http://id.ndl.go.jp/bib/9542150
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I9542150
• Web Site: https://search.jamas.or.jp/link/ui/2008358485
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • CiNii Articles
  • KAKEN
• 抄録ライセンスフラグ: 使用不可