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

Members of the NF-kappa B/rel family of transcription factors are regulated through a trans association with members of a family of inhibitor proteins, collectively known as I kappa B proteins, that contain five to eight copies of a 33-amino-acid repeat sequence (ankyrin repeat). Certain NF-kappa B/rel proteins are also regulated by cis-acting ankyrin repeat-containing domains. The C terminus of p105NF-kappa B, the precursor of the 50-kDa subunit of NF-kappa B, contains a series of ankyrin repeats; proteolytic removal of this ankyrin domain is necessary for the manifestation of sequence-specific DNA binding and nuclear translocation of the N-terminal product. To investigate the structural requirements important for regulation of different NF-kappa B/rel family members by polypeptides containing ankyrin repeat domains, we have constructed a p59v-rel:p105NF-kappa B chimeric protein (p110v-rel-ank). The presence of C-terminal p105NF-kappa B-derived sequences in p110v-rel-ank inhibited nuclear translocation, sequence-specific DNA binding, pp40I kappa B-alpha association, and oncogenic transformation. Sequential truncation of the C-terminal ankyrin domain of p110v-rel-ank resulted in the restoration of nuclear translocation, DNA binding, and pp40I kappa B-alpha association but did not restore the oncogenic properties of p59v-rel. The presence of 67 C-terminal p105NF-kappa B-derived amino acids was sufficient to inhibit both transcriptional activation and oncogenic transformation by p59v-rel. These results support a model in which activation of gene expression by p59v-rel is required for its ability to induce oncogenic transformation.

Heterologous C-terminal sequences disrupt transcriptional activation and oncogenesis by p59v-rel