Point Mutants of Elongation Factor Tu from E. Coli Impaired in Binding Aminoacyl-tRNA

Knudsen, Charlotte R.; Mansilla, Francisco; Pedersen, G.N.; Clark, Brian F. C.

doi:10.1007/978-94-011-4485-8_14

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Sec-trna Sec Interacts With Selb But Not Ef-tu1

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2018

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“…Finally, Sec itself contributes to discrimination of EF-Tu against Sec-tRNA Sec . The amino acid binding pocket of EF-Tu is lined with negatively charged residues [81]. The selenol group of Sec is also negatively charged under physiological conditions [16], and therefore its binding to EF-Tu is disfavored.…”

Section: Sec-trna Sec Interacts With Selb But Not Ef-tumentioning

confidence: 99%

Challenges of site-specific selenocysteine incorporation into proteins byEscherichia coli

Söll

Sevostyanova

2018

RNA Biology

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Selenocysteine (Sec), a rare genetically encoded amino acid with unusual chemical properties, is of great interest for protein engineering. Sec is synthesized on its cognate tRNA (tRNA) by the concerted action of several enzymes. While all other aminoacyl-tRNAs are delivered to the ribosome by the elongation factor Tu (EF-Tu), Sec-tRNA requires a dedicated factor, SelB. Incorporation of Sec into protein requires recoding of the stop codon UGA aided by a specific mRNA structure, the SECIS element. This unusual biogenesis restricts the use of Sec in recombinant proteins, limiting our ability to study the properties of selenoproteins. Several methods are currently available for the synthesis selenoproteins. Here we focus on strategies for in vivo Sec insertion at any position(s) within a recombinant protein in a SECIS-independent manner: (i) engineering of tRNA for use by EF-Tu without the SECIS requirement, and (ii) design of a SECIS-independent SelB route.

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Section: Sec-trna Sec Interacts With Selb But Not Ef-tumentioning

confidence: 99%