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

• Authors: Leszek Tarnowski , Michal Milewski , Jan Fronk , Anna Kurlandzka
• Languages of publication: EN

Abstracts

EN

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.

Keywords

EN

bipartite NLS; nuclear import; SA2 stromalin

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2015
• Volume: 62
• Issue: 2
• Pages: 215-219

Dates

published

2015

received

2014-10-10

revised

2015-03-12

accepted

2015-05-05

(unknown)

2015-05-15

Contributors

author

Leszek Tarnowski

• Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland

author

Michal Milewski

• Department of Medical Genetics, Institute of Mother and Child, Warsaw, Poland

author

Jan Fronk

• Institute of Biochemistry, Faculty of Biology, University of Warsaw, Warsaw, Poland

author

Anna Kurlandzka

• Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland

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Identifiers

DOI

10.18388/abp.2014_915