Interaction of elongation factor 1 with aminoacylated brome mosaic virus and tRNA's

Bastin, Marcel; Hall, Timothy C.

doi:10.1128/jvi.20.1.117-122.1976

Cited by 58 publications

(19 citation statements)

References 28 publications

(29 reference statements)

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“…The remaining 39 host proteins identified with both TBSV and BMV RNA probes are involved in a variety of cellular processes, such as translation initiation or elongation, transcription activation, ribosomal RNA processing/binding, mRNA transport, protein membrane targeting or are predicted to have various biochemical activities, such as helicase, tRNA ligase, tRNA methyltransferase, rRNA dimethylase, ribonuclease, co-chaperone, and protein kinase ( Table 1). One of these proteins, translation elongation factor eEF1A, is the homolog of the plant eEF1A, which has been shown to bind to the BMV RNA (Bastin and Hall, 1976). In addition, the identified pseudouridine synthase Pus4p (Table 1) could be involved in pseudouridynylation--based modification of BMV RNA, which has been shown to occur in vivo (Baumstark and Ahlquist, 2001).…”

Section: Discussionmentioning

confidence: 99%

“…The above protein array-based approach led to the identification of two known BMV RNA binding host proteins (i.e., eEF1A and Pus4p) (Bastin and Hall, 1976;Zhu et al, 2007). However, this approach failed to identify Ded1p and Lsm1p, two known RNA-binding proteins that affected BMV replication in yeast (Diez et al, 2000;Noueiry and Ahlquist, 2003).…”

Section: Usefulness and Limitation Of The Protein Array Approach In Imentioning

confidence: 99%

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Translation elongation factor 1A is a component of the tombusvirus replicase complex and affects the stability of the p33 replication co-factor

Li¹,

Pogany²,

Panavas³

et al. 2009

Virology

122

181

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Host RNA-binding proteins are likely to play multiple, integral roles during replication of plus-strand RNA viruses. To identify host proteins that bind to viral RNAs, we took a global approach based on the yeast proteome microarray, which contains 4080 purified yeast proteins. The biotin-labeled RNA probes included two distantly related RNA viruses, namely Tomato bushy stunt virus (TBSV) and Brome mosaic virus (BMV). Altogether, we have identified 57 yeast proteins that bound to TBSV RNA and/or BMV RNA. Among the identified host proteins, eleven bound to TBSV RNA and seven bound to BMV RNA with high selectivity, whereas the remaining 39 host proteins bound to both viral RNAs. The interaction between the TBSV replicon RNA and five of the identified host proteins were confirmed via gel-mobility shift and co-purification experiments from yeast. Over-expression of the host proteins in yeast, a model host for TBSV, revealed that 4 host proteins that enhanced TBSV replication as well as 14 proteins that inhibited replication. Detailed analysis of one of the identified yeast proteins binding to TBSV RNA, namely translation elongation factor eEF1A, revealed that it is present in the highly purified tombusvirus replicase complex. We also demonstrate binding of eEF1A to the p33 replication protein and a known cis-acting element at the 3′ end of TBSV RNA. Using a functional mutant of eEF1A, we provide evidence on the involvement of eEF1A in TBSV replication.

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Section: Discussionmentioning

confidence: 99%

Section: Usefulness and Limitation Of The Protein Array Approach In Imentioning

confidence: 99%

Translation elongation factor 1A is a component of the tombusvirus replicase complex and affects the stability of the p33 replication co-factor

Li¹,

Pogany²,

Panavas³

et al. 2009

Virology

122

181

View full text Add to dashboard Cite

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“…More detailed experiments with translation elongation factor eEF1A have shown that this host protein is part of the tombusvirus replicase and binds to p33/p92 replication proteins and the 3 0 -UTR of the TBSV (þ)RNA as well. Interestingly, eEF1A has been shown to bind to the BMV RNA (Bastin and Hall, 1976). In addition, the identified pseudouridine synthase Pus4p might be involved in pseudouridinylation-based modification of TBSV RNA and BMV RNA, which has been shown to occur for the BMV RNA in vivo (Baumstark and Ahlquist, 2001).…”

Section: A Yeast Protein Microarray Approach To Identify Host Protmentioning

confidence: 99%

Global Genomics and Proteomics Approaches to Identify Host Factors as Targets to Induce Resistance Against Tomato Bushy Stunt Virus

Nagy

Pogany

2010

Natural and Engineered Resistance to Plant Viruses, Part II

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The success of RNA viruses as pathogens of plants, animals, and humans depends on their ability to reprogram the host cell metabolism to support the viral infection cycle and to suppress host defense mechanisms. Plus-strand (+)RNA viruses have limited coding potential necessitating that they co-opt an unknown number of host factors to facilitate their replication in host cells. Global genomics and proteomics approaches performed with Tomato bushy stunt virus (TBSV) and yeast (Saccharomyces cerevisiae) as a model host have led to the identification of 250 host factors affecting TBSV RNA replication and recombination or bound to the viral replicase, replication proteins, or the viral RNA. The roles of a dozen host factors involved in various steps of the replication process have been validated in yeast as well as a plant host. Altogether, the large number of host factors identified and the great variety of cellular functions performed by these factors indicate the existence of a truly complex interaction between TBSV and the host cell. This review summarizes the advantages of using a simple plant virus and yeast as a model host to advance our understanding of virus-host interactions at the molecular and cellular levels. The knowledge of host factors gained can potentially be used to inhibit virus replication via gene silencing, expression of dominant negative mutants, or design of specific chemical inhibitors leading to novel specific or broad-range resistance and antiviral tools against (+)RNA plant viruses.

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“…One can draw the same conclusion from the recent study (Dreher et al, 1984) performed using brome mosaic virus (BMV) RNA that accepts tyrosine (Kohl and Hall, 1974). Mutations within the 3'-CCA end of BMV RNA preclude aminoacylation [aminoacylation is required for interaction with EF-lac and GTP (Bastin and Hall, 1976)], even though they do not affect replication in vitro.…”

Section: Rna Replicasementioning

confidence: 99%

Interaction of turnip yellow mosaic virus Val-RNA with eukaryotic elongation factor EF-1 [alpha]. Search for a function.

1986

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The 3′‐terminal tRNA‐like structure in turnip yellow mosaic virus (TYMV) RNA can be adenylated by tRNA nucleotidyltransferase and subsequently aminoacylated by valyl‐tRNA synthetase.Here we present evidence that TYMV Val‐RNA can form a stable complex with eukaryotic wheat germ elongation factor EF‐1alpha and GTP: the Val‐RNA is protected by EF‐1alpha.. GTP against digestion by RNase A. By affinity chromatography of TYMV Val‐RNA fragments on immobilized EF‐1alpha . GTP, it has been established that the valylated aminoacyl RNA domain, which in TYMV RNA is formed by the 3′ half of the tRNA‐like region, is sufficient for complex formation with EF‐1alpha . GTP. The aminoacyl RNA domain is equivalent in tRNAs to the continuous helix formed by the acceptor stem and the T stem and loop. In line with these results, the aminoacyl RNA domain in TYMV Val‐RNA complexed to EF‐1 alpha . GTP is resistant to digestion by RNase A. It is also shown that the TYMV RNA replicase (RNA‐dependent RNA polymerase) isolated from TYMV‐infected Chinese cabbage leaves does not contain tRNA nucleotidyltransferase, valyl‐tRNA synthetase or EF‐1alpha. This suggests that interaction of TYMV RNA with EF‐1alpha is not mandatory for replicase activity.

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Interaction of elongation factor 1 with aminoacylated brome mosaic virus and tRNA's

Cited by 58 publications

References 28 publications

Translation elongation factor 1A is a component of the tombusvirus replicase complex and affects the stability of the p33 replication co-factor

Translation elongation factor 1A is a component of the tombusvirus replicase complex and affects the stability of the p33 replication co-factor

Global Genomics and Proteomics Approaches to Identify Host Factors as Targets to Induce Resistance Against Tomato Bushy Stunt Virus

Interaction of turnip yellow mosaic virus Val-RNA with eukaryotic elongation factor EF-1 [alpha]. Search for a function.

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