Serine-173 of the Epstein-Barr-Virus Zebra Protein Is Required for DNA-Binding and Is a Target for Casein Kinase-Ii Phosphorylation

Kolman, J. L., Taylor, N., Marshak, D. R., Miller, G. (November 1993) Serine-173 of the Epstein-Barr-Virus Zebra Protein Is Required for DNA-Binding and Is a Target for Casein Kinase-Ii Phosphorylation. Proc Natl Acad Sci U S A, 90 (21). pp. 10115-10119. ISSN 0027-8424

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Abstract

An Epstein-Barr virus-encoded protein, ZEBRA, mediates the switch from latency to the viral lytic life cycle. ZEBRA's domain structure and DNA binding specificity resemble that of cellular transcriptional activators such as c-Fos/c-Jun. We show that ZEBRA, like c-Jun, is phosphorylated by casein kinase II (CKII). The principal site of phosphorylation is serine-173 (S173), five amino acids upstream of the basic DNA recognition domain. CKII phosphorylation abrogated ZEBRA's capacity to bind its target DNA sequences. S173 is a functional component of ZEBRA's DNA binding domain, since mutation of S173 to alanine (S173A) reduced DNA binding in vitro to 10% of wild-type levels. Transcriptional activation of a native viral promoter in vivo by mutant S173A was also reduced markedly. Reversible phosphorylation of S173 is likely to be an important means of regulating ZEBRA's activity in vivo.

Item Type: Paper
Uncontrolled Keywords: SERUM RESPONSE FACTOR BZLF1 PROMOTER EARLY ANTIGEN CELL-GROWTH TRANSACTIVATOR EXPRESSION ACTIVATION SITES TRANSCRIPTION REGIONS
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > transcription
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > c-fos
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > c-jun
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > oncogene
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor
CSHL Authors:
Communities: CSHL labs
Depositing User: Matt Covey
Date: 1 November 1993
Date Deposited: 07 Apr 2016 18:57
Last Modified: 09 Nov 2017 19:42
PMCID: PMC47724
Related URLs:
URI: https://repository.cshl.edu/id/eprint/32595

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