Distinct genetic code expansion strategies for selenocysteine and pyrrolysine are reflected in different aminoacyl-tRNA formation systems

Jing Yuan; Patrick O’Donoghue; Alex Ambrogelly; Sarath Gundllapalli; R. Lynn Sherrer; Sotiria Palioura; Miljan Simonović; Dieter Söll

doi:10.1016/j.febslet.2009.11.005

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Distinct genetic code expansion strategies for selenocysteine and pyrrolysine are reflected in different aminoacyl-tRNA formation systems

Journal article

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Distinct genetic code expansion strategies for selenocysteine and pyrrolysine are reflected in different aminoacyl-tRNA formation systems

Jing Yuan, Patrick O’Donoghue, Alex Ambrogelly, Sarath Gundllapalli, R. Lynn Sherrer, Sotiria Palioura, Miljan Simonović and Dieter Söll

FEBS letters, Vol.584(2), pp.342-349

2010

DOI: https://doi.org/10.1016/j.febslet.2009.11.005

PMCID: PMC2795046

PMID: 19903474

Abstract

o-phosphoseryl-tRNA Sec kinase

Sep-tRNA:Sec-tRNA synthase

Pyrrolysyl-tRNA synthetase

Natural suppression

Stop codon re-coding

Selenocysteine and pyrrolysine, known as the 21st and 22nd amino acids, are directly inserted into growing polypeptides during translation. Selenocysteine is synthesized via a tRNA-dependent pathway and decodes UGA (opal) codons. The incorporation of selenocysteine requires the concerted action of specific RNA and protein elements. In contrast, pyrrolysine is ligated directly to tRNA Pyl and inserted into proteins in response to UAG (amber) codons without the need for complex re-coding machinery. Here we review the latest updates on the structure and mechanisms of molecules involved in Sec-tRNA Sec and Pyl-tRNA Pyl formation as well as the distribution of the Pyl-decoding trait.

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Collaboration types: Industry collaboration; Domestic collaboration
Citation topics: 2 Chemistry; 2.170 Nucleic Acids Chemistry; 2.170.185 Ribosome
Web Of Science research areas: Biochemistry & Molecular Biology; Biophysics; Cell Biology
ESI research areas: Biology & Biochemistry

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Title: Distinct genetic code expansion strategies for selenocysteine and pyrrolysine are reflected in different aminoacyl-tRNA formation systems
Creators: Jing Yuan - Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA
Patrick O’Donoghue - Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA
Alex Ambrogelly - Schering-Plough Corporation, Kenilworth, NJ 07033-0530, USA
Sarath Gundllapalli - Schering-Plough Corporation, Kenilworth, NJ 07033-0530, USA
R. Lynn Sherrer - Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA
Sotiria Palioura - Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA
Miljan Simonović - Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL 60607, USA
Dieter Söll - Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA
Publication Details: FEBS letters, Vol.584(2), pp.342-349
Publisher: Elsevier B.V
Academic Unit: UMMG Department of Ophthalmology
Language: English
Resource Type: Journal article
PMID: 19903474
PMCID: PMC2795046
Record Identifier: 991031600952202976