Ribosomal initiation from an ACG codon in the Sendai virus P/C mRNA.

Curran, Joseph; Kolakofsky, Daniel

doi:10.1002/j.1460-2075.1988.tb02806.x

Cited by 179 publications

(137 citation statements)

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“…The P mRNA, however, has been demonstrated to be polycistronic. In addition to encoding the 568 amino acid (aa) P protein, it also codes for a pair of non-structural proteins, C (204 aa) and C' (181 aa) (Curran et al, 1986;Dethlefsen & Kolakofsky, 1983;Giorgi et al, 1983) which represent a C-coterminal nested set and are derived from an overlapping open reading frame (ORF) (see Fig. 1).…”

Section: Discussionmentioning

confidence: 99%

“…2) also shows that the major translation product of the P mRNA in vitro is the C protein, as is the case in vivo (Curran et al, 1986), although this effect appears exaggerated in this in vitro reaction. The C' protein is also visible among the in vitro translation products whereas a separate C' protein cannot be detected among the in vivo proteins (lane 2).…”

mentioning

confidence: 87%

“…Although it is possible that undetectable amounts of C' protein were made during this viral infection, it is also possible that the two C proteins are comigrating in the gel, as has previously been shown to occur under some conditions. [The C' protein is actually 26 aa shorter than the C protein and the reason for its aberrant slower migration than the C protein on some gels is unknown (Curran et al, 1986).] Finally, lane 5 (Fig.…”

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confidence: 99%

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Identification of an Additional Sendai Virus Non-structural Protein Encoded by the P/C mRNA

Curran¹,

Kolakofsky

1987

Journal of General Virology

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SUMMARYPeptide antiserum and monoclonal antibodies have detected a previously unrecognized small non-structural protein in Sendai virus-infected cells. This protein, designated X, appears to represent the C-terminal 95 amino acids of the P protein reading frame. The X protein appears to be almost as abundant as the P protein on a molar basis in vivo. No evidence of a precursor-product relationship between the X and P proteins could be found.Sendai virus, a member of the parainfluenza virus genus of the paramyxovirus family, encodes its entire genetic information within a non-segmented 15 kb negative strand (-) RNA genome (Kingsbury, 1974;Kolakofsky et al., 1974). Upon infection, this genetic information is expressed via positive-sense mRNAs transcribed from the-genome by the virion-associated polymerase. These transcripts are largely monocistronic, encoding the NP, M, F, HN and L proteins. The P mRNA, however, has been demonstrated to be polycistronic. In addition to encoding the 568 amino acid (aa) P protein, it also codes for a pair of non-structural proteins, C (204 aa) and C' (181 aa) (Curran et al., 1986;Dethlefsen & Kolakofsky, 1983;Giorgi et al., 1983) which represent a C-coterminal nested set and are derived from an overlapping open reading frame (ORF) (see Fig. 1). The C overlapping ORF has also been conserved in the closely related human parainfluenza virus 3 (Spriggs & Collins, 1986a) as well as the two morbilliviruses examined to date, measles virus and canine distemper virus (Barrett et al., 1985;Bellini et al., 1985). Curiously, in the case of the parainfluenza viruses simian virus 5, Newcastle disease virus and mumps virus, non-structural proteins are again encoded within the P mRNA, but here these non-structural proteins appear to share tryptic peptides with the P protein and are therefore thought to be encoded by the same ORF (Collins et al., 1982;Herrler & Compans, 1982;Paterson et al., 1984). Only in the case of respiratory syncytial virus, a member of the more distinctly related pneumovirus genus, is the P mRNA thought to be monocistronic (Collins et al., 1984).Recently, Herman (1986) has found that the NS mRNA of the rhabdovirus vesicular stomatitis virus (VSV), which is thought to be the VSV equivalent of the parainfluenza virus P mRNA, also codes for a second small protein, representing the C-terminal 62 aa of the 265 aa long NS protein. Since the Sendal virus P protein and the VSV NS protein have several characteristics in common, and antiserum specific for the C-terminal t6 aa of the Sendai virus P protein is available, we examined whether the same also applies to Sendai virus.Sendai virus (Harris strain)-infected BHK cells were labelled for 2 h at 18 h post-infection, when marked cytopathic effects are apparent, as well as a parallel uninfected culture. Under these conditions, host protein synthesis has largely been displaced by the viral protein synthesis and the virus structural proteins and the non-structural C protein can clearly be detected above the remaining cellular background ...

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Section: Discussionmentioning

confidence: 99%

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confidence: 87%

mentioning

confidence: 99%

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Identification of an Additional Sendai Virus Non-structural Protein Encoded by the P/C mRNA

Curran¹,

Kolakofsky

1987

Journal of General Virology

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“…Although this is generally the case there is a growing body of evidence that non-AUG codons can also serve as initiation codons. This was first demonstrated in viruses (Curran and Kolakofsky, 1988), but since, initiation of translation at non-AUG codons has also been observed with mammalian mRNAs. In their review Touriol et al list 15 mRNAs for which initiation at non-AUG codons has been demonstrated.…”

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confidence: 78%

An insight into the post‐transcriptional control of gene expression in cell function

Osborne

2003

Biology of the Cell

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“…The non-AUG-initiated product is often the less abundant of the two (11,36,47). The functional relevance of the non-AUG-initiated polypeptides has not often been demonstrated.…”

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confidence: 99%

Non-AUG Initiation ofAGAMOUSmRNA Translation inArabidopsis thaliana

Riechmann

Ito

Meyerowitz

1999

Molecular and Cellular Biology

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The MADS box organ identity gene AGAMOUS (AG) controls several steps during Arabidopsis thaliana flower development. AG cDNA contains an open reading frame that lacks an ATG triplet to function as the translation initiation codon, and the actual amino terminus of the AG protein remains uncharacterized. We have considered the possibility that AG translation can be initiated at a non-AUG codon. Two possible non-AUG initiation codons, CUG and ACG, are present in the 5 region of AG mRNA preceding the highly conserved MADS box sequence. We prepared a series of AG genomic constructs in which these codons are mutated and assayed their activity in phenotypic rescue experiments by introducing them as transgenes into ag mutant plants. Alteration of the CTG codon to render it unsuitable for acting as a translation initiation site does not affect complementation of the ag-3 mutation in transgenic plants. However, a similar mutation of the downstream ACG codon prevents the rescue of the ag-3 mutant phenotype. Conversely, if an ATG is introduced immediately 5 to the disrupted ACG codon, the resulting construct fully complements the ag-3 mutation. The AG protein synthesized in vitro by initiating translation at the ACG position is active in DNA binding and is of the same size as the AG protein detected from floral tissues, whereas AG polypeptides with additional amino-terminal residues do not appear to bind DNA. These results indicate that translation of AG is initiated exclusively at an ACG codon and prove that non-AUG triplets may be efficiently used as the sole translation initiation site in some plant cellular mRNAs.

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Ribosomal initiation from an ACG codon in the Sendai virus P/C mRNA.

Cited by 179 publications

References 20 publications

Identification of an Additional Sendai Virus Non-structural Protein Encoded by the P/C mRNA

Identification of an Additional Sendai Virus Non-structural Protein Encoded by the P/C mRNA

An insight into the post‐transcriptional control of gene expression in cell function

Non-AUG Initiation ofAGAMOUSmRNA Translation inArabidopsis thaliana

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