Genomic RNA of mengovirus V. Recognition of common features by ribosomes and eucaryotic initiation factor 2

Perez-Bercoff, R.; Kaempfer, Raymond

doi:10.1128/jvi.41.1.30-41.1982

Cited by 48 publications

(15 citation statements)

References 59 publications

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“…Indeed, it has been shown (1, 14, 23, 32) that on a molar basis, mengovirus mRNA competes 35 times more effectively in translation than does globin mRNA; that is, half-maximal inhibition of globin synthesis occurred in lysates that contained 35 molecules of globin mRNA for every molecule of mengovirus RNA. Also, mengovirus mRNA binds eIF-2 with a 30-fold-higher affinity than globin mRNA (29,32). These observations suggest that under limiting conditions of protein synthesis, mengovirus mRNA may still be translated to a sufficient degree for progeny virus formation.…”

Section: Discussionmentioning

confidence: 99%

Evidence for the presence of an inhibitor on ribosomes in mouse L cells infected with mengovirus

Pensiero¹,

Lucas‐Lenard²

1985

J Virol

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After infection of mouse L cells with mengovirus, there is a rapid inhibition of protein synthesis, a concurrent disaggregation of polysomes, and an accumulation of 80S ribosomes. These 80S ribosomes could not be chased back into polysomes under an elongation block. The infected-cell 8OS-ribosome fraction contained twice as much initiator methionyl-tRNA and mRNA as the analogous fraction from uninfected cells. Since the proportion of 80S ribosomes that were resistant to pronase digestion also increased after infection, these data suggest that the accumulated 80S ribosomes may be in the form of initiation complexes. The specific protein synthetic activity of polysomal ribosomes also decreased with time of infection. However, the transit times in mock-infected and infected cells remained the same. Cell-free translation systems from infected cells reflected the decreased protein synthetic activity of intact cells. The addition of reticulocyte initiation factors to such systems failed to relieve the inhibition. Fractionation of the infected-cell lysate revealed that the ribosomes were the predominant target affected. Washing the infected-cell ribosomes with 0.5 M KCI restored their translational activity. In turn, the salt wash from Infected-cell ribosomes inhibited translation in lysates from mock-infected cells. The inhibitor in the ribosomal salt wash was temperature sensitive and micrococcal nuclease resistant. A model is proposed wherein virus infection activates (or induces the synthesis of) an inhibitor that binds to ribosomes and stops translation after the formation of the 8OS-ribosome initiation complex but before elongation. The presence of such an inhibitor on ribosomes could prevent them from being remobilized into polysomes in the presence of an inhibitor of polypeptide elongation.

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Section: Discussionmentioning

confidence: 99%

Evidence for the presence of an inhibitor on ribosomes in mouse L cells infected with mengovirus

Pensiero¹,

Lucas‐Lenard²

1985

J Virol

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“…In fact, the fingerprints obtained upon terminal RNase T1 digestion of the fragments associated with either the 80S or the 40S initiation complexes in lysates of control or IFNtreated cells were just undistinguishable. The complexity of the pattern observed and the previous location of these oligonucleotides in two clusters of the RNA molecule (17) suggested that the in vitro translation of picornavirus RNA involved a novel mechanism of initiation.…”

mentioning

confidence: 95%

“…These results, however, left unanswered the major issue regarding the ability of ribosomes of IFN-treated cells to recognize and interact with the proper areas of the mRNA. Accordingly, the fragments of 32P-labeled mengovirus RNA selected for by ribosomes of IFN-treated cells at initiation of translation were isolated and fingerprinted by procedures fully described elsewhere (17). Four large T1-resistant oligonucleotides were obtained upon terminal digestion with RNase T1 of the fragments of mengovirus RNA protected in the 80S initiation complexes formed in lysates of untreated L-cells (Fig.…”

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confidence: 99%

“…Fingerprint analysis of the sequences of 32P-labeled mengovirus RNA recognized by ribosomes of control and IFN-treated L-cells at initiation of translation. 32P-labeled mengovirus RNA was incubated under conditions allowing initiation of translation (17). The fragments of 32P-labeled mengovirus RNA protected against nuclease attack in the initiation complexes were isolated, extracted, and fingerprinted as described previously (17).…”

mentioning

confidence: 99%

“…32P-labeled mengovirus RNA was incubated under conditions allowing initiation of translation (17). The fragments of 32P-labeled mengovirus RNA protected against nuclease attack in the initiation complexes were isolated, extracted, and fingerprinted as described previously (17). T1 fingerprints of the sequences of 32P-labeled mengovirus RNA recovered from the 80S initiation complexes formed in lysates of IFN-treated (A) or control (B) L-cells.…”

mentioning

confidence: 99%

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Genomic RNA of mengovirus. VI. Translation of its two cistrons in lysates of interferon-treated cells

Degener¹,

Pagnotti²,

Facchini³

et al. 1983

J Virol

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The addition of low levels (40 ng/ml) of the synthetic double-stranded polyribonucleotide poly I:C to lysates of interferon-treated L-cells resulted in a strong inhibition (70 to 75%) of the in vitro translation of mengovirus RNA. Under these conditions, the rates of incorporation of [35S]methionine or formyl-[35S]methionine were depressed to a comparable extent. The sequences of mengovirus RNA recognized by ribosomes of interferon-treated cells at initiation of translation were compared with those present in initiation complexes formed by ribosomes of untreated controls. Fingerprint analysis revealed that the same sequences of mengovirus RNA were protected against nuclease attack by the 80S and the 40S initiation complexes formed in vitro in lysates of control or interferon-treated L-cells. Mengovirus RNA-coded proteins were labeled at their N-terminal end with formyl-[35S]methionine and digested to completion with trypsin. The resulting fragments were separated by high-voltage paper electrophoresis. Two different formyl-[35S]methionine-labeled N termini were resolved. Further analyses supported the notion that the two radioactive peaks originated in the initiation of translation at two different sites. This pattern did not change when mengovirus RNA was translated in lysates of interferon-treated cells.

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Genetic Engineering of Animal Cells

Wirth¹,

Hauser²

1992

Biotechnology

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Genomic RNA of mengovirus V. Recognition of common features by ribosomes and eucaryotic initiation factor 2

Cited by 48 publications

References 59 publications

Evidence for the presence of an inhibitor on ribosomes in mouse L cells infected with mengovirus

Evidence for the presence of an inhibitor on ribosomes in mouse L cells infected with mengovirus

Genomic RNA of mengovirus. VI. Translation of its two cistrons in lysates of interferon-treated cells

Genetic Engineering of Animal Cells

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