Functionality of the STNV translational enhancer domain correlates with affinity for two wheat germ factors

Lipzig, Rosalinde van; Montagu, Marc Van; Cornelissen, Marc; Meulewaeter, Frank

doi:10.1093/nar/29.5.1080

Cited by 11 publications

(17 citation statements)

References 25 publications

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“…The 120-nucleotide fragment of 18 S rRNA does not cross-link to subunits of either complex (lanes 4 -6). These results confirm that the proteins in wheat germ extract that UV cross-link to STNV-2 TED reported by van Lipzig et al (53) are subunits of eIF-4F and eIF(iso)4F.…”

Section: Figsupporting

confidence: 91%

“…The STNV-2 TED was recently shown by van Lipzig et al (53) in UV-cross-linking assays to bind 28-and 30-kDa proteins in wheat germ extracts (53). These proteins were not identified but were suggested to correspond to the plant cap-binding proteins eIF4E and eIF(iso)4E (53). Further deletion studies more finely mapped the 5Ј and 3Ј boundaries of the STNV-2 TED (54).…”

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confidence: 97%

“…These results suggest that the tertiary structure of the viral RNA may be important for maximal cap independence. The STNV-2 TED was recently shown by van Lipzig et al (53) in UV-cross-linking assays to bind 28-and 30-kDa proteins in wheat germ extracts (53). These proteins were not identified but were suggested to correspond to the plant cap-binding proteins eIF4E and eIF(iso)4E (53).…”

mentioning

confidence: 97%

“…Several models for ribosomal recruitment by the STNV TED have been proposed, including base pairing to 18 S rRNA, base pairing of the 5Ј and 3Ј-UTRs and direct recruitment of a component(s) of the translational apparatus (49,(51)(52)(53)(54). Given the profound effects of the STNV-1 TED on eIF4F requirement (49), it seems likely that eIF4F is directly involved in the cap-independent translation of this viral RNA.…”

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confidence: 99%

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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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Section: Figsupporting

confidence: 91%

mentioning

confidence: 97%

mentioning

confidence: 97%

mentioning

confidence: 99%

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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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“…The genomic RNAs of many viruses lack a poly(A) tail, and elements in the 5Ј and͞or 3Ј UTR are believed to compensate for the absence of a poly(A) tail (8)(9)(10)(11)(12). Recently, the rotavirus (family Reoviridae) NSP3 protein was shown to interact with eIF-4G and with the 3Ј UTR of the nonpolyadenylated viral mRNAs.…”

mentioning

confidence: 99%

Translation of a nonpolyadenylated viral RNA is enhanced by binding of viral coat protein or polyadenylation of the RNA

Neeleman

Olsthoorn²,

Linthorst³

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

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C ircularization of the genome of RNA viruses plays an essential role in the replication and translation of viral RNAs. Formation of panhandle structures by base pairing between complementary sequences at the 5Ј and 3Јtermini of several genera of minus-strand RNA viruses has been known already for some time (1). Recently, it became clear that cyclization by RNA-RNA interactions may also play an essential role in the replication of positive-strand RNA viruses such as f laviviruses (2, 3). However, for a growing number of positive-strand RNA viruses, circularization seems to be mediated by protein bridges between the 5Ј and 3Ј termini of the viral RNA. On entry into the host cell, the genome of positive-strand RNA viruses has to serve as messenger for the translation of viral proteins including replication factors. A number of viral RNAs resemble cellular mRNAs by having a 5Ј-cap structure (m 7 GpppN) and 3Ј-poly(A) tail. In cellular mRNAs, these structures permit the formation of a protein bridge by interactions between eIF4G and eIF4E from the cap-binding complex of translation initiation factors and the poly(A) binding protein (PABP) associated with the poly(A) tail (4, 5). Picornaviruses do not have a cap structure, but the internal ribosome entry site in the 5Ј untranslated region (UTR) of the RNA binds initiation factors and a poly(rC) binding protein that mediate the interaction with PABP. Circularization of Poliovirus RNA seems to play a role both in translation and replication of the viral RNA (6, 7).The genomic RNAs of many viruses lack a poly(A) tail, and elements in the 5Ј and͞or 3Ј UTR are believed to compensate for the absence of a poly(A) tail (8-12). Recently, the rotavirus (family Reoviridae) NSP3 protein was shown to interact with eIF-4G and with the 3Ј UTR of the nonpolyadenylated viral mRNAs. Both interactions were required for efficient translation of the viral mRNA, and NSP3 was suggested to mimic the function of PABP (13). Here, we report evidence that the coat protein (CP) of alfalfa mosaic virus (AMV; genus Alfamovirus, family Bromoviridae) also may act as a functional equivalent of PABP.RNAs 1 and 2 of the tripartite AMV genome encode the replicase proteins P1 and P2, respectively. P1 contains methyltransferase-and helicase-like motifs, whereas P2 contains polymerase-like motifs. RNA 3 encodes the movement protein and CP, which is translated from a subgenomic messenger, RNA 4. The RNAs contain a 5Ј-cap structure but the 3Ј ends are not polyadenylated (14). At their 3Ј termini, RNAs 1-4 contain a homologous sequence of 145 nucleotides that can be folded into two alternative conformations: a linear array of hairpins with flanking AUGC sequences that represents a strong CP binding site or a tRNA-like structure that represents the promoter for minus-strand RNA synthesis (15). A mixture of the three genomic RNAs becomes infectious only after addition of CP or its messenger, RNA 4, to the inoculum (16). Initiation of infection requires binding of a few molecules of CP to the 3Ј termini of the g...

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Effective non‐viral leader for cap‐independent translation in a eukaryotic cell‐free system

Shaloiko

Granovsky

Ивашина

et al. 2004

Biotech & Bioengineering

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The 61 nt 5'-untranslated region (5'-UTR) of mRNA encoding for a light-emitting protein of hydroid polyp Obelia longissima, obelin, is shown to provide a high level of cap-independent translation of heterologous mRNAs in cell-free translation systems based on wheat germ extracts. The inhibition of translation typically observed when excess mRNA is present or produced in a eukaryotic system (the so-called self-inhibition phenomenon) is found abated with mRNA constructs carrying the obelin mRNA leader. The role of the sequestration of a limiting initiation factor, probably eIF4F, in the self-inhibition phenomenon and the possible independence of the obelin mRNA leader from eIF4F are discussed. We propose the obelin mRNA leader be used for effective cap-independent translation in eukaryotic cell-free systems, including combined transcription-translation systems with uncontrolled phage polymerase-catalyzed accumulation of mRNA.

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Functionality of the STNV translational enhancer domain correlates with affinity for two wheat germ factors

Cited by 11 publications

References 25 publications

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

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

Translation of a nonpolyadenylated viral RNA is enhanced by binding of viral coat protein or polyadenylation of the RNA

Effective non‐viral leader for cap‐independent translation in a eukaryotic cell‐free system

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