Skip Navigation

This Article
Right arrow Print PDF (8444K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (10)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Tyler, J. K.
Right arrow Articles by Everett, R. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tyler, J. K.
Right arrow Articles by Everett, R. D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1994, Vol. 22, No. 5 711-721
© 1994

MOLECULAR BIOLOGY

The DNA binding domains of the varicella-zoster virus gene 62 and herpes simplex virus type 1 ICP4 transactivator proteins heterodimerize and bind to DNA

Jessica K. Tyler and Roger D. Everett*

MRC Virology Unit Church Street, Glasgow G11 5JR, UK

*To whom correspondence should be addressed

Received December 24, 1993. Revised February 1, 1994. Accepted February 1, 1994.

The product of varicella-zoster virus gene 62 (VZV 140k) Is the functional counterpart of the major transcrlptional regulatory protein of herpes simplex virus type 1 (HSV-1), ICP4. We have found that the purified bacterlally expressed DNA blnding domain of VZV 140k (residues 417–647) is a stable dimer in solution. As demonstrated by the appearance of a novel protein -DNA complex of intermediate mobility in gel retardation assays, following In vitro co-translation of a pair of differently sized VZV 140k DNA binding domain peptides, the 140k DNA binding domain peptide binds to DNA as a dimer. In addition, the DNA binding domain peptides of HSV-1 ICP4 readily heterodimerizes with the VZV 140k peptide on co-translation, Indicating that HSV-1 ICP4 and VZV 140k possess very similar dimerization interfaces. It appears that only one fully wild type subunit of the dimer is sufficient to mediate sequence specific DNA recognition in certain circumstances. Co-lmmunopreclpitation analysis of mutant DNA binding domain peptides, co-translated with an epitope-tagged ICP4 DNA binding domain, shows that the sequence requirements for dimerlzation are lower than those necessary for DNA binding.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Virol.Home page
M. Yang, H. Peng, J. Hay, and W. T. Ruyechan
Promoter Activation by the Varicella-Zoster Virus Major Transactivator IE62 and the Cellular Transcription Factor USF.
J. Virol., August 1, 2006; 80(15): 7339 - 7353.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
B. Sato, H. Ito, S. Hinchliffe, M. H. Sommer, L. Zerboni, and A. M. Arvin
Mutational Analysis of Open Reading Frames 62 and 71, Encoding the Varicella-Zoster Virus Immediate-Early Transactivating Protein, IE62, and Effects on Replication In Vitro and in Skin Xenografts in the SCID-hu Mouse In Vivo
J. Virol., May 15, 2003; 77(10): 5607 - 5620.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
M. H. Sommer, E. Zagha, O. K. Serrano, C. C. Ku, L. Zerboni, A. Baiker, R. Santos, M. Spengler, J. Lynch, C. Grose, et al.
Mutational Analysis of the Repeated Open Reading Frames, ORFs 63 and 70 and ORFs 64 and 69, of Varicella-Zoster Virus
J. Virol., September 1, 2001; 75(17): 8224 - 8239.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.