The major transcriptional regulatory protein of herpes simplex virus type 1 includes a protease resistant DNA binding domain

Everett, R.D., Paterson, T. and Elliott, M. (1990) The major transcriptional regulatory protein of herpes simplex virus type 1 includes a protease resistant DNA binding domain. Nucleic Acids Research, 18(15), pp. 4579-4585. (doi:10.1093/nar/18.15.4579)

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Abstract

Herpes simplex virus type 1 expresses five immediateearly (IE) polypeptides. In the absence of functional Vmw175 (the product of IE gene 3) activation of transcription of later classes of viral genes and repression of IE gene expression does not occur. The recognition of specific DNA sequences by Vmw175 requires, as determined by sensitivity to mutation, a part of the protein highly conserved in the corresponding proteins of related herpes viruses. However, mutations in other parts of the protein can also disrupt specific DNA binding. This paper shows that the DNA binding domain of Vmw175 can be liberated as a functional unit by digestion with proteinase K. Analysis of mutant Vmw175 proteinsshowed that the proteinase K resistant domain has an amino terminus between amino acid residues 229 and 292, while its carboxy terminus is between residues 495 and 518. Mutations outside this region which affect DNA binding by the intact protein do not eliminate binding of the proteinase K resistant domain. This implies that direct DNA binding by Vmw175 involves a linear subsection of the polypeptide, and that mutations in other parts of the polypeptide which affect DNA binding of the whole protein do so by indirect means.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Everett, Professor Roger
Authors: Everett, R.D., Paterson, T., and Elliott, M.
College/School:College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
Journal Name:Nucleic Acids Research
Publisher:Oxford University Press
ISSN:0305-1048
ISSN (Online):1362-4962
Copyright Holders:Copyright © 1990 Oxford University Press
First Published:First published in Nucleic Acids Research 18(15):4579-4585
Publisher Policy:Reproduced in accordance with the copyright policy of the publisher

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