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. 1991 Jan;65(1):206–212. doi: 10.1128/jvi.65.1.206-212.1991

The promoter, transcriptional unit, and coding sequence of herpes simplex virus 1 family 35 proteins are contained within and in frame with the UL26 open reading frame.

F Y Liu 1, B Roizman 1
PMCID: PMC240506  PMID: 1845885

Abstract

The herpes simplex virus 1 (HSV-1) genome specifies an abundant capsid protein which in denaturing gels forms multiple bands designated family 35 proteins (D.K. Braun, B. Roizman, and L. Pereira, J. Virol. 49:142-153, 1984). Nucleotide-sequencing studies have assigned the coding sequences of these proteins to the open reading frame UL26 (D.J. McGeoch, M.A. Dalrymple, A.J. Davidson, A. Dolan, M.C. Frame, D. McNab, L.J. Perry, J.E. Scott, and P. Taylor, J. Gen. Virol. 69:1531-1574, 1988). IN studies reported here, a series of plasmid constructs containing deletions or insertions of an alpha 4 promoter or of a sequence encoding a cytomegalovirus epitope reacting with a mouse monoclonal antibody revealed the following: the open reading frame previously designated UL26 encodes two proteins which share amino acid sequences, and each coding domain is contained in its own transcriptional unit that terminates at a common, unique poly(A) site. On the basis of the transcription initiation site (+1), it was predicted that the UL26 open reading frame encodes a protein of 635 amino acids, and a protein with an apparent molecular weight of approximately 75,000 has been identified. The second transcriptional unit, designated UL26.5, predicted to specify a protein of 329 amino acids, encodes the family 35 proteins; it is transcribed by an mRNA which initiates at approximately nucleotide +1000 of the UL26 transcription initiation site and is translated from the methionine initiation codon located at position +1099 of the UL26 transcriptional unit. The DNA fragment comprising the sequences downstream of the HpaI cleavage site (+832 of UL26) contains both the promoter and the coding sequence of family 35 proteins and is both competent and efficient in expressing the proteins in transfected cells superinfected with HSV-1 or HSV-2.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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