Molecular mechanism of selenoprotein P synthesis
Selenoprotein synthesis requires the reinterpretation of a UGA stop codon as one that encodes selenocysteine (Sec), a process that requires a set of dedicated translation factors. Among the mammalian selenoproteins, Selenoprotein P (SELENOP) is unique as it contains a selenocysteine-rich domain that...
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Published in | Biochimica et biophysica acta. General subjects Vol. 1862; no. 11; pp. 2506 - 2510 |
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Main Authors | , |
Format | Journal Article |
Language | English |
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Elsevier B.V
01.11.2018
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Abstract | Selenoprotein synthesis requires the reinterpretation of a UGA stop codon as one that encodes selenocysteine (Sec), a process that requires a set of dedicated translation factors. Among the mammalian selenoproteins, Selenoprotein P (SELENOP) is unique as it contains a selenocysteine-rich domain that requires multiple Sec incorporation events.
In this review we elaborate on new data and current models that provide insight into how SELENOP is made.
SELENOP synthesis requires a specific set of factors and conditions.
As the key protein required for proper selenium distribution, SELENOP stands out as a lynchpin selenoprotein that is essential for male fertility, proper neurologic function and selenium metabolism.
•Selenoprotein synthesis requires the reinterpretation of a UGA stop codon as one that encodes selenocysteine (Sec).•Selenoprotein P (SELENOP) is unique as it contains a selenocysteine-rich domain that requires multiple Sec incorporation events.•SELENOP synthesis requires a unique set of factors and RNA structures.•SELENOP is essential for male fertility, proper neurologic function and selenium metabolism. |
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AbstractList | Selenoprotein synthesis requires the reinterpretation of a UGA stop codon as one that encodes selenocysteine (Sec), a process that requires a set of dedicated translation factors. Among the mammalian selenoproteins, Selenoprotein P (SELENOP) is unique as it contains a selenocysteine-rich domain that requires multiple Sec incorporation events.BACKGROUNDSelenoprotein synthesis requires the reinterpretation of a UGA stop codon as one that encodes selenocysteine (Sec), a process that requires a set of dedicated translation factors. Among the mammalian selenoproteins, Selenoprotein P (SELENOP) is unique as it contains a selenocysteine-rich domain that requires multiple Sec incorporation events.In this review we elaborate on new data and current models that provide insight into how SELENOP is made.SCOPE OF REVIEWIn this review we elaborate on new data and current models that provide insight into how SELENOP is made.SELENOP synthesis requires a specific set of factors and conditions.MAJOR CONCLUSIONSSELENOP synthesis requires a specific set of factors and conditions.As the key protein required for proper selenium distribution, SELENOP stands out as a lynchpin selenoprotein that is essential for male fertility, proper neurologic function and selenium metabolism.GENERAL SIGNIFICANCEAs the key protein required for proper selenium distribution, SELENOP stands out as a lynchpin selenoprotein that is essential for male fertility, proper neurologic function and selenium metabolism. Selenoprotein synthesis requires the reinterpretation of a UGA stop codon as one that encodes selenocysteine (Sec), a process that requires a set of dedicated translation factors. Among the mammalian selenoproteins, Selenoprotein P (SELENOP) is unique as it contains a selenocysteine-rich domain that requires multiple Sec incorporation events. In this review we elaborate on new data and current models that provide insight into how SELENOP is made. SELENOP synthesis requires a specific set of factors and conditions. As the key protein required for proper selenium distribution, SELENOP stands out as a lynchpin selenoprotein that is essential for male fertility, proper neurologic function and selenium metabolism. •Selenoprotein synthesis requires the reinterpretation of a UGA stop codon as one that encodes selenocysteine (Sec).•Selenoprotein P (SELENOP) is unique as it contains a selenocysteine-rich domain that requires multiple Sec incorporation events.•SELENOP synthesis requires a unique set of factors and RNA structures.•SELENOP is essential for male fertility, proper neurologic function and selenium metabolism. Selenoprotein synthesis requires the reinterpretation of a UGA stop codon as one that encodes selenocysteine (Sec), a process that requires a set of dedicated translation factors. Among the mammalian selenoproteins, Selenoprotein P (SELENOP) is unique as it contains a selenocysteine-rich domain that requires multiple Sec incorporation events.In this review we elaborate on new data and current models that provide insight into how SELENOP is made.SELENOP synthesis requires a specific set of factors and conditions.As the key protein required for proper selenium distribution, SELENOP stands out as a lynchpin selenoprotein that is essential for male fertility, proper neurologic function and selenium metabolism. Selenoprotein synthesis requires the reinterpretation of a UGA stop codon as one that encodes selenocysteine (Sec), a process that requires a set of dedicated translation factors. Among the mammalian selenoproteins, Selenoprotein P (SELENOP) is unique as it contains a selenocysteine-rich domain that requires multiple Sec incorporation events. In this review we elaborate on new data and current models that provide insight into how SELENOP is made. SELENOP synthesis requires a specific set of factors and conditions. As the key protein required for proper selenium distribution, SELENOP stands out as a lynchpin selenoprotein that is essential for male fertility, proper neurologic function and selenium metabolism. |
Author | Copeland, Paul R. Shetty, Sumangala |
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Snippet | Selenoprotein synthesis requires the reinterpretation of a UGA stop codon as one that encodes selenocysteine (Sec), a process that requires a set of dedicated... |
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SubjectTerms | male fertility mammals metabolism SBP2 SECIS SECISBP2L Selenium Selenocysteine Selenoprotein P selenoproteins stop codon translation (genetics) |
Title | Molecular mechanism of selenoprotein P synthesis |
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