The unique tRNA Sec and its role in selenocysteine biosynthesis.
Autor: | Serrão VHB; São Carlos Institute of Physics, University of São Paulo, São Carlos, Brazil.; Neurobiology Department, Harvard Medical School, Boston, USA., Silva IR; São Carlos Institute of Physics, University of São Paulo, São Carlos, Brazil., da Silva MTA; São Carlos Institute of Physics, University of São Paulo, São Carlos, Brazil., Scortecci JF; São Carlos Institute of Physics, University of São Paulo, São Carlos, Brazil., de Freitas Fernandes A; São Carlos Institute of Physics, University of São Paulo, São Carlos, Brazil., Thiemann OH; São Carlos Institute of Physics, University of São Paulo, São Carlos, Brazil. thiemann@ifsc.usp.br.; Department of Genetics and Evolution, Federal University of São Carlos, São Carlos, Brazil. thiemann@ifsc.usp.br. |
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Jazyk: | angličtina |
Zdroj: | Amino acids [Amino Acids] 2018 Sep; Vol. 50 (9), pp. 1145-1167. Date of Electronic Publication: 2018 Jun 12. |
DOI: | 10.1007/s00726-018-2595-6 |
Abstrakt: | Selenium (Se) is an essential trace element for several organisms and is mostly present in proteins as L-selenocysteine (Sec or U). Sec is synthesized on its L-seryl-tRNA Sec to produce Sec-tRNA Sec molecules by a dedicated selenocysteine synthesis machinery and incorporated into selenoproteins at specified in-frame UGA codons. UGA-Sec insertion is signaled by an mRNA stem-loop structure called the SElenoCysteine Insertion Sequence (SECIS). tRNA Sec transcription regulation and folding have been described showing its importance to Sec biosynthesis. Here, we discuss structural aspects of Sec-tRNA Sec and its role in Sec biosynthesis as well as Sec incorporation into selenoproteins. Defects in the Sec biosynthesis or incorporation pathway have been correlated with pathological conditions. |
Databáze: | MEDLINE |
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