Structure and function of a cap-independent translation element that functions in either the 3′ or the 5′ untranslated region

Guo, Liang; Allen, Edwards; Miller, W. Allen

doi:10.1017/s1355838200001539

Cited by 86 publications

(159 citation statements)

References 69 publications

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“…Instead of a cap and poly(A) tail interacting synergistically, BYDV has a BYDV translation element (BTE) located in the 3Ј-UTR that interacts with a stem loop in the 5Ј-UTR of its mRNA (20,21). The 3Ј BTE comprises nucleotides 4814 -4918, has a cruciform/tRNA-like secondary structure with three major stem-loops (SL-I, SL-II, and SL-III) with stem loop IV forming the base, and is the minimum requirement for successful in vitro translation (see Fig.…”

Section: Barley Yellow Dwarf Virus (Bydv)mentioning

confidence: 99%

“…The 3Ј BTE comprises nucleotides 4814 -4918, has a cruciform/tRNA-like secondary structure with three major stem-loops (SL-I, SL-II, and SL-III) with stem loop IV forming the base, and is the minimum requirement for successful in vitro translation (see Fig. 1) (20). Cap-independent translation initiation at the upstream AUG is stimulated by 3Ј BTE via base pairing (kissing stem loop interaction) of the 3Ј SL-III to the 5Ј SL-D loop of the viral genomic RNA (see Fig.…”

Section: Barley Yellow Dwarf Virus (Bydv)mentioning

confidence: 99%

“…In this study, WT 3Ј BTE and four other mutants BTEBF, SII-m1, SL-III-3, and SL-III SWAP (the mutations/changes in bases are shown in Fig. 1) with in vitro translation efficiencies from 5 to 164% compared with WT BTE (2,20) were used. Binding of eIF4F and other initiation factors (eIF4B, 4A, and PABP) to the WT 3Ј BTE and mutants (BTEBF, SII-m1, SL-III-3, and SL-III SWAP) was characterized using fluorescence anisotropy and stopped flow kinetics, which gave equilibrium binding constant values (K d ), a measure of relative complex stability, and kinetic constants.…”

Section: Barley Yellow Dwarf Virus (Bydv)mentioning

confidence: 99%

“…To further examine what, if any, role binding of eIF4F had on translation, a variety of 3Ј BTE mutants with widely different translational efficiencies were selected for binding studies. 3Ј BTE and mutants with in vitro translation efficiencies from 5 to 164% (WT ϭ 100%) were studied (2,20). All of the mutants contain a short 17-nucleotide-long sequence (located in SL-I) conserved across viral classes, which is the location for eIF4F binding and is complementary to 18S ribosomal RNA (24,33).…”

Section: Translation Efficiencies Of 3ј Bte and Mutants Correlatementioning

confidence: 99%

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Eukaryotic Initiation Factor (eIF) 4F Binding to Barley Yellow Dwarf Virus (BYDV) 3′-Untranslated Region Correlates with Translation Efficiency

Banerjee

Goss

2014

Journal of Biological Chemistry

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Background:Little is known about BYDV protein synthesis initiation mechanisms. Results: eIF4F binding correlates with 3Ј BTE translation efficiency and is enthalpically and entropically favorable. Conclusion: Binding of eIF4F to the 3Ј BTE is important for efficient BYDV translation. Significance: Binding of eIF4F to the 3Ј-UTR to initiate assembly of the protein synthesis initiation complex is a novel mechanism that may be used by other viruses containing a 3Ј BTE.

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Section: Barley Yellow Dwarf Virus (Bydv)mentioning

confidence: 99%

Section: Barley Yellow Dwarf Virus (Bydv)mentioning

confidence: 99%

Section: Barley Yellow Dwarf Virus (Bydv)mentioning

confidence: 99%

Section: Translation Efficiencies Of 3ј Bte and Mutants Correlatementioning

confidence: 99%

See 2 more Smart Citations

Eukaryotic Initiation Factor (eIF) 4F Binding to Barley Yellow Dwarf Virus (BYDV) 3′-Untranslated Region Correlates with Translation Efficiency

Banerjee

Goss

2014

Journal of Biological Chemistry

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“…The addition of the BYDV TE domain in trans specifically inhibits in vitro translation and is reversed by the addition of eIF4F (39). The BYDV TE has been shown to interact through base pairing with a stem-loop located in the 5Ј-UTR (40,41), serving as a way for the viral RNA to bring the 5Ј-and 3Ј-UTRs into contact mimicking the eIF4G-PABP interaction.…”

mentioning

confidence: 99%

A Novel Interaction of Cap-binding Protein Complexes Eukaryotic Initiation Factor (eIF) 4F and eIF(iso)4F with a Region in the 3′-Untranslated Region of Satellite Tobacco Necrosis Virus

Gazo

Murphy

Gatchel

et al. 2004

Journal of Biological Chemistry

108

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Satellite tobacco necrosis virus (STNV)RNA is naturally uncapped at its 5 end and lacks polyadenylation at its 3 end. Despite lacking these two hallmarks of eukaryotic mRNAs, STNV-1 RNA is translated very efficiently. A ϳ130-nucleotide translational enhancer (TED), located 3 to the termination codon, is necessary for efficient cap-independent translation of STNV-1 RNA. The STNV-1 TED RNA fragment binds to the eukaryotic cap-binding complexes, initiation factor (eIF) 4F and eIF(iso)4F, as measured by nitrocellulose binding and fluorescence titration. STNV-1 TED is a potent inhibitor of in vitro translation when added in trans. This inhibition is reversed by the addition of eIF4F or eIF(iso)4F, and the subunits of eIF4F and eIF(iso)4F cross-link to STNV-1 TED, providing additional evidence that these factors interact directly with STNV-1 TED. Deletion mutagenesis of the STNV-1 TED indicates that a minimal region of ϳ100 nucleotides is necessary to promote cap-independent translation primarily through interaction with the cap binding subunits (eIF4E or eIF(iso)4E) of eIF4F or eIF(iso)4F.Initiation of protein synthesis in eukaryotic cells is a complicated process requiring 8 -10 initiation factors for proper alignment of the initiation codon of messenger RNA on the 40 S ribosome and subsequent joining of the 60 S ribosome (for review, see Refs. 1-6). For eukaryotes the first step in this process is the recognition of the m 7 GpppX cap structure at the 5Ј end of mRNA by eIF4E, 1 the cap-binding protein component of the eIF4F complex. The eIF4G component of eIF4F then acts as a scaffold for the assembly of other initiation factors (for review, see Refs. 7-11). Initiation factors eIF4A, eIF3, and poly(A)-binding protein (PABP) are known to interact with eIF4G during this process (for review, see Refs. 7, 9, and 10). PABP binds the poly(A) tail present at the 3Ј end of most cellular mRNAs, and the interaction of PABP with eIF4G implies that the 5Ј and 3Ј ends of the cellular mRNA are brought into close proximity during the initiation process (for review, see Refs. 9 and 12). This assembly of factors on the mRNA presumably functions in an ATP-dependent unwinding of secondary structure in the 5Ј-UTR of the mRNA before binding and scanning of the 40 S ribosome to find the correct initiation codon (5).Plant eIF4F consists of two subunits, a small cap-binding protein, eIF4E (26 kDa), and a large subunit, eIF4G (180 kDa). Higher plants possess an isozyme form of eIF4F, termed eIF(iso) 4F (13, 14). eIF(iso)4F, like eIF4F, consists of two subunits, eIF(iso)4E (28 kDa), and a large subunit, eIF(iso)4G (86 kDa). eIF(iso)4F has functions similar to eIF4F in the initiation of translation of plant mRNAs (14). The amino acid sequence of plant eIF(iso)4E is ϳ50% similar to plant eIF4E and retains all the conserved tryptophan residues found in cap-binding proteins (15,16). The large subunit, eIF(iso)4G, is significantly smaller than plant eIF4G (86 versus 180 kDa, (15)), sharing ϳ30 -40% similarity with central and C-terminal regions o...

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In Vivo Translation Studies of Plant Viral RNAs Using Reporter Genes

Matsuda

Dreher

2005

CP Microbiology

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This unit describes the analysis of the translation‐regulating properties of viral RNAs in cell‐based assays using a luciferase reporter system. Electroporation and polyethylene glycol–mediated introduction of luciferase reporter RNA into cowpea protoplasts are also presented. The Commentary section discusses employing the luciferase reporter system to study translational control by the 5′‐ and 3′‐untranslated regions of a viral mRNA. Inoculum RNA quality and half‐life after delivery to the protoplasts should be monitored closely for careful investigation of translational regulation elements.

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Structure and function of a cap-independent translation element that functions in either the 3′ or the 5′ untranslated region

Cited by 86 publications

References 69 publications

Eukaryotic Initiation Factor (eIF) 4F Binding to Barley Yellow Dwarf Virus (BYDV) 3′-Untranslated Region Correlates with Translation Efficiency

Eukaryotic Initiation Factor (eIF) 4F Binding to Barley Yellow Dwarf Virus (BYDV) 3′-Untranslated Region Correlates with Translation Efficiency

A Novel Interaction of Cap-binding Protein Complexes Eukaryotic Initiation Factor (eIF) 4F and eIF(iso)4F with a Region in the 3′-Untranslated Region of Satellite Tobacco Necrosis Virus

In Vivo Translation Studies of Plant Viral RNAs Using Reporter Genes

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