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J. Virol., 12 1995, 7648-7657, Vol 69, No. 12
IK Ruf and DR Rawlins
The transition from latency to lytic Epstein-Barr virus replication is
dependent on the Epstein-Barr virus BZLF1 gene product. Genetic and
biochemical attempts to link cellular second-messenger signaling pathways
that trigger this transition with the subsequent viral gene cascade have
identified functional elements within the BZLF1 promoter (Zp) that appear
to bind undefined cellular transcription factors. One of these previously
identified sites, ZII, has homology to consensus AP- 1 and CREB binding
sites, implying a role for these factors in the inductive process. We have
identified and characterized ZIIBC, a ZII site binding complex that is
distinct from the factors previously proposed to bind this site. Active
ZIIBC was found to be present in both uninduced and chemically induced cell
extracts at approximately equivalent concentrations. Analysis of the DNA
sequence requirements for the binding of ZIIBC to the ZII site shows that
sequences homologous to AP-1 and CREB consensus sites are necessary but not
sufficient for complex formation. Although the components of ZIIBC that
directly contact DNA were found to be of the same molecular masses (26 and
36 kDa) in both uninduced and chemically induced cell extracts, a slight
mobility difference between DNA-protein complexes formed by these two types
of extracts is observable and indicates that ZIIBC is directly affected by
chemical induction. The effects of ZIIBC binding to the ZII site on
expression from Zp were evaluated, and they suggest that ZIIBC plays a
critical role in the regulation of Zp expression.
Copyright © 1995, American Society for Microbiology
Identification and characterization of ZIIBC, a complex formed by cellular factors and the ZII site of the Epstein-Barr virus BZLF1 promoter
Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
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