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New biologic functions--selenium-dependent nucleic acids and proteins.

T C Stadtman

    Fundamental and Applied Toxicology : Official Journal of the Society of Toxicology
    |September 1, 1983
    PubMed
    Summary
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    Selenium is a vital component in enzymes and transfer RNAs (tRNAs) across organisms. Its presence, particularly as selenocysteine and selenomethionine in selenoenzymes and specific tRNAs, is crucial for biological functions.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Microbiology

    Background:

    • Selenium is an essential trace element incorporated into specific proteins and nucleic acids in living organisms.
    • Selenoenzymes and selenium-modified transfer RNAs (tRNAs) play critical roles in various biological processes.
    • The biosynthesis of bacterial selenoenzymes is independent of sulfur levels.

    Purpose of the Study:

    • To identify and characterize selenium-containing biomolecules in bacterial and animal systems.
    • To elucidate the chemical forms of selenium within identified selenoenzymes and seleno-tRNAs.
    • To investigate the functional significance of selenium in tRNA structure and activity.

    Main Methods:

    • Isolation and characterization of selenoenzymes and selenoproteins from bacterial and animal sources.

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  • Chemical analysis to determine the specific selenium-containing forms (selenocysteine, selenomethionine, or other derivatives).
  • Identification and analysis of selenium-modified nucleosides in specific tRNAs, including structural and functional assays.

    • Main Results:

    • Identified bacterial selenoenzymes include glycine reductase, formate dehydrogenases, hydrogenase, nicotinic acid hydroxylase, xanthine dehydrogenase, and thiolase.
    • Selenocysteine is the predominant selenium form in many enzymes, while selenomethionine occurs in bacterial thiolase.
    • A unique selenium-modified nucleoside, 5-methyl-aminomethyl-2-selenouridine (mnm5Se2U), was identified in glutamate and lysine isoaccepting tRNAs.
    • Loss of selenium from mnm5Se2U in tRNA resulted in loss of glutamate charging activity, highlighting selenium's essential role.

    Conclusions:

    • Selenium is incorporated into diverse biomolecules, including enzymes and tRNAs, across different life forms.
    • The specific chemical forms of selenium vary, with selenocysteine and selenomethionine being common in enzymes.
    • Selenium modification of tRNA, particularly the mnm5Se2U nucleoside, is essential for amino acid charging activity and likely plays a role in synthetase-tRNA recognition.