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 Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

In contrast to our understanding of the roles of Oct-1 and VP16 in VP16-mediated transcriptional activation, virtually nothing is known of the role of the second cellular component, termed host cell factor (HCF), or of its structure-function relationships. We show that the majority of the internal region of HCF, including the repeats involved in HCF cleavage, is dispensable for complex assembly with VP16 and Oct-1. The N-terminal domain of HCF (HCF.N) had only weak VP16 binding and complex promoting activity, while the C-terminal region (HCF.C) had no intrinsic activity. However, the C-terminal region strongly enhanced complex formation and reduced dissociation kinetics when linked to the N-terminal domain (HCF.NC). The potent activity of the HCF.NC fusion in complex assembly was recapitulated in vivo in yeast and mammalian cells. Moreover, HCF.N could promote increased complex formation when the acidic activation domain of VP16 was deleted. Restoration of the activation domain strongly inhibited complex formation with HCF.N, but the addition of the C-terminal domain of HCF restored strong stable complex formation with intact VP16. The results indicate that this C-terminal domain is critically required to alter the presentation of the acidic domain of VP16. Additional results are consistent with the interpretation that this alteration in acidic domain presentation for complex assembly also facilitates the activation function in VP16. The sequence of an HCF homolog from Caenorhabditis elegans shows it to be a natural HCF.NC construct, reinforcing the conclusions from our functional analysis.

molecular and cellular biology

Concerted Activity of Host Cell Factor Subregions in Promoting Stable VP16 Complex Assembly and Preventing Interference by the Acidic Activation Domain