SECIS binding proteins and eukaryotic selenoprotein synthesis

Donna M. Driscoll; Paul R. Copeland

doi:10.1007/0-387-33827-6_6

SECIS binding proteins and eukaryotic selenoprotein synthesis

Donna M. Driscoll, Paul R. Copeland

Robert Wood Johnson Medical School (RWJMS), Biochemistry & Molecular Biology

Research output: Chapter in Book/Report/Conference proceeding › Chapter

1 Scopus citations

Abstract

In eukaryotes, the biosynthesis of selenoproteins involves a novel translational mechanism that recodes UGA as selenocysteine (See). The decision to incorporate Sec rather than terminate protein synthesis involves at least two RNA-binding proteins that interact specifically with a conserved motif within the 3' untranslated region (3' UTR) of the selenoprotein mRNA. The structures, functions, and interactions of these two proteins, SECIS Binding Protein 2 (SBP2) and ribosomal protein L30 (L30), are considered in detail in this chapter.

Original language	English (US)
Title of host publication	Selenium
Subtitle of host publication	Its Molecular Biology and Role in Human Health, Second Edition
Publisher	Springer US
Pages	63-72
Number of pages	10
ISBN (Electronic)	9780387338279
ISBN (Print)	0387338268, 9780387338262
DOIs	https://doi.org/10.1007/0-387-33827-6_6
State	Published - 2006

All Science Journal Classification (ASJC) codes

Medicine(all)

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10.1007/0-387-33827-6_6

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AB - In eukaryotes, the biosynthesis of selenoproteins involves a novel translational mechanism that recodes UGA as selenocysteine (See). The decision to incorporate Sec rather than terminate protein synthesis involves at least two RNA-binding proteins that interact specifically with a conserved motif within the 3' untranslated region (3' UTR) of the selenoprotein mRNA. The structures, functions, and interactions of these two proteins, SECIS Binding Protein 2 (SBP2) and ribosomal protein L30 (L30), are considered in detail in this chapter.

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PB - Springer US

ER -

SECIS binding proteins and eukaryotic selenoprotein synthesis

Abstract

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