Selenium Toxicity: Aminoacylation and Peptide Bond Formation with Selenomethionine

Autor:	Alex Shrift, David C. Eustice, Fredrick J. Kull
Rok vydání:	1981
Předmět:	Methionine Physiology Chemistry Stereochemistry food and beverages chemistry.chemical_element Translation (biology) Aminoacylation Articles Plant Science Ribosome In vitro chemistry.chemical_compound Biochemistry Genetics Protein biosynthesis Peptide bond Selenium
Zdroj:	Plant Physiology. 67:1054-1058
ISSN:	1532-2548 0032-0889
DOI:	10.1104/pp.67.5.1054
Popis:	Selenomethionine and methionine were compared as substrates for in vitro aminoacylation, ribosome binding, and peptide bond formation with preparations from wheat germ. Selenomethionine paralleled methionine in all steps of the translation process except peptide bond formation. Peptide bond formation with the initiating species of tRNA(Met) demonstrated that selenomethionyl-tRNA(Met) was less effective as a substrate than was methionyl-tRNA(f) (Met). Participation of selenomethionine in the initiation process of translation could be expected to reduce the overall rate of protein synthesis and might aid in explaining selenium toxicity in selenium-sensitive plants.
Databáze:	OpenAIRE
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