Structure. 2007 May;15(5):577-86.

Structural basis for dynamic interdomain movement and RNA recognition of the selenocysteine-specific elongation factor SelB.

Ose T, Soler N, Rasubala L, Kuroki K, Kohda D, Fourmy D, Yoshizawa S, Maenaka K.

Source

Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, Fukuoka 812-8582, Japan.

Abstract

Selenocysteine (Sec) is the "21st" amino acid and is genetically encoded by an unusual incorporation system. The stop codon UGA becomes a Sec codon when the selenocysteine insertion sequence (SECIS) exists downstream of UGA. Sec incorporation requires a specific elongation factor, SelB, which recognizes tRNA(Sec) via use of an EF-Tu-like domain and the SECIS mRNA hairpin via use of a C-terminal domain (SelB-C). SelB functions in multiple translational steps: binding to SECIS mRNA and tRNA(Sec), delivery of tRNA(Sec) onto an A site, GTP hydrolysis, and release from tRNA and mRNA. However, this dynamic mechanism remains to be revealed. Here, we report a large domain rearrangement in the structure of SelB-C complexed with RNA. Surprisingly, the interdomain region forms new interactions with the phosphate backbone of a neighboring RNA, distinct from SECIS RNA binding. This SelB-RNA interaction is sequence independent, possibly reflecting SelB-tRNA/-rRNA recognitions. Based on these data, the dynamic SelB-ribosome-mRNA-tRNA interactions will be discussed.

PMID:: 17502103; [PubMed - indexed for MEDLINE]

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Research Support, Non-U.S. Gov't

MeSH Terms

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Secondary Source ID

PDB/2UWM

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Cited by 3 PubMed Central articles

Thermodynamic and kinetic framework of selenocysteyl-tRNASec recognition by elongation factor SelB. [J Biol Chem. 2010]
Thermodynamic and kinetic framework of selenocysteyl-tRNASec recognition by elongation factor SelB.
Paleskava A, Konevega AL, Rodnina MV. J Biol Chem. 2010 Jan 29; 285(5):3014-20. Epub 2009 Nov 23.
The selenoproteome of Clostridium sp. OhILAs: characterization of anaerobic bacterial selenoprotein methionine sulfoxide reductase A. [Proteins. 2009]
The selenoproteome of Clostridium sp. OhILAs: characterization of anaerobic bacterial selenoprotein methionine sulfoxide reductase A.
Kim HY, Zhang Y, Lee BC, Kim JR, Gladyshev VN. Proteins. 2009 Mar; 74(4):1008-17.
The three-dimensional structure of the Moorella thermoacetica selenocysteine insertion sequence RNA hairpin and its interaction with the elongation factor SelB. [RNA. 2007]
The three-dimensional structure of the Moorella thermoacetica selenocysteine insertion sequence RNA hairpin and its interaction with the elongation factor SelB.
Beribisky AV, Tavares TJ, Amborski AN, Motamed M, Johnson AE, Mark TL, Johnson PE. RNA. 2007 Nov; 13(11):1948-56. Epub 2007 Sep 27.

Structures reported by this article

C-Terminal Domain(Wh2-Wh4) Of Elongation Factor Selb In Complex With Secis Rna

PDB: 2UWM

Source: Moorella thermoacetica

Method: X-Ray Diffraction

Resolution: 2.31 Å

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