Protein Synthesis in Sendai Virus-infected Cells

Zaides, V. M.; Selimova, L. M.; Жирнов, О. П.; Bukrinskaya, A. G.

doi:10.1099/0022-1317-27-3-319

Cited by 17 publications

(7 citation statements)

References 16 publications

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“…For both VSV and Sendai virus, the primacy of transcriptional regulation of polypeptide abundances need not be absolute. A superimposed "fine-tuning" level of translational control has not been disproven; in fact, close inspection of our data on the relative abundance of the putative message for polypeptide L compared with available data on the abundance of polypeptide L in infected cells (24,38) suggests that this message is inefficiently translated. A similar situation may exist for the L polypeptide of VSV (15).…”

Section: Discussionmentioning

confidence: 71%

Regulation of Sendai virus transcription: evidence for a single promoter in vivo

Glazier¹,

Raghow²,

Kingsbury³

1977

J Virol

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The synthesis of Sendai virus RNA species was examined after UV irradiation of cells late in infection. Compared with the inactivation of 50S genomic RNA synthesis, the synthesis of the group of mRNA species that sediments at 18S was inactivated at an average rate consistent with a process of sequential transcription from a single promoter. The rates of inactivation of the synthesis of individual mRNA's separated by polyacrylamide gel electrophoresis confirmed this and, with the aid of additional data, suggested that the order of genes in the Sendai virus genome is: 3'-NP-Fo-M-P-HM-L-5'.

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Section: Discussionmentioning

confidence: 71%

Regulation of Sendai virus transcription: evidence for a single promoter in vivo

Glazier¹,

Raghow²,

Kingsbury³

1977

J Virol

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“…Perhaps only one of the forms of P is a component of the transcriptase, whereas most of P may have other roles. Recently, V. Chinchar and A. Portner (personal communication) found that Sendai nucleocapsids containing a 40-kilodalton proteolytic fragment of P retained most of their enzymatic activity, suggesting either a greater enzymatic role for the L protein (19,52) or that only part of the P molecule is required.…”

Section: T: 'mentioning

confidence: 99%

Identification of the P proteins and other disulfide-linked and phosphorylated proteins of Newcastle disease virus

Smith¹,

Hightower²

1981

J Virol

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A unique abundant protein, designated P by analogy to the putative polymerase proteins of other paramyxoviruses, was identified in purified Newcastle disease virus. Under nonreducing conditions the P proteins could be separated from other viral proteins on sodium dodecyl sulfate-polyacrylamide gels. The P proteins were isolated from detergent-solubilized virions as 53,000to 55,000-dalton monomers and disulfide-linked trimers. Distinct forms of P having four-different isoelectric points and two different electrophoretic mobilities were resolved by two-dimensional electrophoresis. Two forms of P were phosphorylated, as were the nucleocapsid protein and non-glycosylated membrane protein. In addition to disulfidelinked forms of P, dimers of the hemagglutinin-neuraminidase glycoprotein and two disulfide-linked versions of the fusion glycoprotein were identified. Several electrophoretic variants of the nucleocapsid protein that were probably created by intrachain disulfide bonding were also isolated from virions under nonreducing conditions. The locations of the newly identified proteins were determined by detergent-salt fractionation of virions and by surface-selective radioiodination of the viral envelope. The P proteins were associated with nucleocapsids and were not detected at the surface of virions. Both forms of the fusion glycoproteins were on the exterior of the viral envelope. Herein the properties of the P proteins are compared with similar proteins of rhabdoviruses and other paramyxoviruses, and a role for multiple forms of proteins in the genetic economy of Newcastle disease virus is discussed.

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“…The heavily exposed auto radiograms ( fig. 1) reveal several minor polypeptide species, which have also been described before [13,14], One of these, designated L, has recently been identified as a nucleocapsid component [12][13][14], It has a molecular weight of about 160,000 and it is apparently specified by a large (33S) messenger RNA species [13,15]. Unfortunately, considering its probable relevance to Sendai virus nucleocapsid functions, it was present in insufficient amounts in our preparations to permit tryptic peptide analyses.…”

mentioning

confidence: 95%

“…The labeled virion and nucleocapsid polypeptides were resolved in typical fashion by discontinuous SDS-PAGE [11][12][13][14] as shown in figure 1. The major virion polypeptides, P, HN , F", NP.…”

mentioning

confidence: 99%