English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

In herpes simplex virus (HSV)-infected cells, viral gene expression is initiated when the immediate-early, or alpha, genes are transactivated by the alpha gene trans-inducing factor (alpha TIF), a component of the infecting virion. The protein binds to one or more recognition elements (TAATGARAT) in the promoters of alpha genes via interaction with the cellular proteins Oct-1 and CFF. The alpha TIF of HSV (HSV-alpha TIF) is believed to subsequently accelerate the assembly of the transcription complex by direct contact between its carboxyl-terminal acidic activation domain and at least two components of the transcription apparatus, TAFII40 and TFIIB. Like its HSV counterpart, the alpha TIF of bovine herpesvirus (BHV) (designated BHV-alpha TIF) also transactivates alpha gene promoters and for full activity exhibits a requirement for its extended carboxyl-terminal region. Despite this requirement, there is a notable lack of homology to the carboxyl-terminal acidic activation domain of HSV-alpha TIF. We swapped the amino- and carboxyl-terminal domains of HSV-alpha TIF and BHV-alpha TIF to make chimeric proteins. Using these chimeras, we show that the carboxyl terminus of BHV-alpha TIF is insufficient for transactivation, which requires cooperative determinants in both the amino-terminal and carboxyl-terminal regions of the protein. We have previously shown that the amino-terminal determinant in BHV-alpha TIF displays reduced but significant independent transactivation potential. Interestingly, this amino-terminal determinant appears not to reside in the HSV-alpha TIF, which displays no independent amino-terminal activity. Furthermore, we show that the amino-terminal activation domain of BHV-alpha TIF may be able to act synergistically with the carboxyl-terminal activation domain of HSV-alpha TIF, since a chimeric protein containing both domains appeared to be more efficient at activating transcription than either alpha TIF. In addition, the amino terminus of HSV-alpha TIF could not restore activity when linked to the carboxyl terminus of BHV-alpha TIF, while the amino terminus of BHV-alpha TIF reconstituted an intact protein with potent activation potential. We also show that in fusions with the DNA binding domain of GAL4, full activity requires the entire BHV-alpha TIF, although both amino and carboxyl termini display some activity on their own. In contrast, for HSV-alpha TIF, the carboxyl terminus is sufficient and possibly even more potent than the entire protein, while the amino-terminus is devoid of activity.(ABSTRACT TRUNCATED AT 400 WORDS)

journal of virology

The bovine herpesvirus alpha gene trans-inducing factor activates transcription by mechanisms different from those of its herpes simplex virus type 1 counterpart VP16