Mutation of a single lysine residue severely impairs the DNA recognition and regulatory functions of the VZV gene 62 transactivator protein

Tyler, J.T., Allen, K.E. and Everett, R.D. (1994) Mutation of a single lysine residue severely impairs the DNA recognition and regulatory functions of the VZV gene 62 transactivator protein. Nucleic Acids Research, 22(3), pp. 270-278. (doi:10.1093/nar/22.3.270)

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Abstract

The product of varicella-zoster virus gene 62 (VZV 140k) Is a potent transactivator protein. We have Identified a region within the DNA binding domain of VZV 140k that shows a striking similarity to the DNA recognition helix of the homeodomain, with an especially highly conserved quartet of residues, WLQN. The 140k protein has functional counterparts within the other alphaherpesvlruses, which Include the major transcrlptlonal regulatory protein of HSV-1, (ICP4), and the WLQN region is highly conserved among the members of this family of viral transactlvators. Substitution of VZV 140k residue lysine 548, just adjacent to the WLQN region, drastically reduces the DNA binding activity of the 140k DNA binding domain and the Intact 140k mutant protein fails to activate gene expression. Substitutions of two other VZV 140k residues in this conserved WLQN region result In alterations to the DNA binding Interaction and reduced transactivation activities. All three mutations act at the level of DNA recognition, as they have no apparent effect on the dimerizatlon state, solubility or efficiency of expression of the mutant peptides.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Everett, Professor Roger
Authors: Tyler, J.T., Allen, K.E., and Everett, R.D.
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 © 1994 Oxford University Press
First Published:First published in Nucleic Acids Research 22(3): 270-278
Publisher Policy:Reproduced in accordance with the copyright policy of the publisher

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