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

Stromalins are evolutionarily conserved multifunctional proteins with the best known function in sister chromatid cohesion. Human SA2 stromalin, likely involved in the establishment of cohesion, contains numerous potential nuclear localization (NLS) and nuclear export signals (NES). Previously we have found that the C-terminus of SA2 contains NLS(s) functional in human cells. However, the identity of this signal remained unclear since three NLS-like sequences are present in that region. Here we analyzed the functionality of these putative signals by expressing GFP-tagged C-terminal part of SA2 or its fragments in a human cell line and in the yeast Saccharomyces cerevisiae. We found that in human cells the nuclear import is dependent on a unique compound di- or tripartite signal containing unusually long linkers between clusters of basic amino acids. Upon expression of the same SA2 fragment in yeast this signal is also functional and can be easily studied in more detail.

A compound C-terminal nuclear localization signal of human SA2 stromalin