Capsid protein precursor is one of two initiated products of translation of poliovirus RNA in vitro

Humphries, Suzanne; Knauert, F; Ehrenfeld, E

doi:10.1128/jvi.30.2.481-488.1979

Cited by 19 publications

(8 citation statements)

References 24 publications

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“…They are also consistent with the proposal (17) that the polymerase precursor C donates VPg to the nascent RNA strand during initiation of synthesis. G016) 1 (11) i(9)() 4. Processing map of EMC viral proteins revised to include proteins H and VPg.…”

Section: Resultsmentioning

confidence: 99%

“…(Nomenclature for polioviral protein is that of Summers et al [24] as modified by Butterworth [1], and that for encephalomyocarditis [EMC] viral proteins is that of Butterworth et al [2].) Alternatively, it has been suggested that VPg may represent the product of a less frequently translated second cistron (11). There is, however, no direct evidence supporting either of these proposals.…”

mentioning

confidence: 99%

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Picornaviral VPg sequences are contained in the replicase precursor

Pallansch¹,

Kew²,

Palmenberg³

et al. 1980

J Virol

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It has previously been shown that the RNA replicase of encephalomyocarditis virus contains two virus-coded proteins, D and E, which are produced in two successive proteolytic steps: (i) C-D + ?; and (ii) D-* p22 + E. It is here shown (i) that virus protein H (molecular weight, 12,000) is the previously unidentified product of the first step and (ii) that VPg, a protein linked covalently to the virion RNA, yields two tryptic peptides found in protein C but not in protein D. The results suggest that VPg is derived by cleavage of protein C and that protein H may be an intermediate. Preliminary experiments with VPg sequences in polioviral noncapsid protein lb, the counterpart of encephalomyocarditis viral protein C, were inconclusive.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Picornaviral VPg sequences are contained in the replicase precursor

Pallansch¹,

Kew²,

Palmenberg³

et al. 1980

J Virol

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“…1). The second formyl methioninelabeled polypeptide has not been identified yet (106), but it was produced in lysates programmed with defective-interfering particle RNA, indicating its lack of relatedness to NCVP la.…”

Section: Number Of Initiation Sitesmentioning

confidence: 99%

Picornaviral structure and assembly.

Putnak¹,

Phillips²

1981

Microbiological Reviews

117

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“…In N-formyl-[35S]methionine labeling studies, including tryptic peptide analysis, two proteins synthesized from independent initiation events have been identified in both the reticulocyte lysate and the poliovirus-infected HeLa cell extract programmed with poliovirus RNA (3,12). In these studies, utilization of the two different initiation sites on the RNA was modulated by the concentration of magnesium.…”

mentioning

confidence: 99%

In vitro translation of poliovirus RNA: utilization of internal initiation sites in reticulocyte lysate

Dorner¹,

Semler²,

Jackson³

et al. 1984

J Virol

230

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The translation of poliovirus RNA in rabbit reticulocyte lysate was examined. Translation of poliovirus RNA in this cell-free system resulted in an electrophoretic profile of poliovirus-specific proteins distinct from that observed in vivo or after translation in poliovirus-infected HeLa cell extract. A group of proteins derived from the P3 region of the polyprotein was identified by immunoprecipitation, time course, and Nformyl-V35S]methionine labeling studies to be the product of the initiation of protein synthesis at an internal site(s) located within the 3'-proximal RNA sequences. Utilization of this internal initiation site(s) on poliovirus RNA was abolished when reticulocyte lysate was supplemented with poliovirus-infected HeLa cell extract. Authentic P1-la was also synthesized in reticulocyte lysate, indicating that correct 5'-proximal initiation of translation occurs in that system. We conclude that the deficiency of a component(s) of the reticulocyte lysate necessary for 5'-proximal initiation of poliovirus protein synthesis resulted in the ability of ribosomes to initiate translation on internal sequences. This aberrant initiation could be corrected by factors present in the HeLa cell extract. Apparently, under certain conditions, ribosomes are capable of recognizing internal sequences as authentic initiation sites.

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Capsid protein precursor is one of two initiated products of translation of poliovirus RNA in vitro

Cited by 19 publications

References 24 publications

Picornaviral VPg sequences are contained in the replicase precursor

Picornaviral VPg sequences are contained in the replicase precursor

Picornaviral structure and assembly.

In vitro translation of poliovirus RNA: utilization of internal initiation sites in reticulocyte lysate

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