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Cell Death Differ. 2016 Nov 1;23(11):1739-1748. doi: 10.1038/cdd.2016.93. Epub 2016 Sep 9.

Tudor staphylococcal nuclease: biochemistry and functions.

Author information

1
Department of Chemistry and Biotechnology, Uppsala BioCenter, Swedish University of Agricultural Sciences and Linnean Center for Plant Biology, Uppsala, Sweden.
2
Faculty of Basic Medicine, MV Lomonosov Moscow State University, Moscow, Russia.
3
Division of Toxicology, Institute of Environmental Medicine, Karolinska Institutet, Stockholm, Sweden.

Abstract

Tudor staphylococcal nuclease (TSN, also known as Tudor-SN, SND1 or p100) is an evolutionarily conserved protein with invariant domain composition, represented by tandem repeat of staphylococcal nuclease domains and a tudor domain. Conservation along significant evolutionary distance, from protozoa to plants and animals, suggests important physiological functions for TSN. It is known that TSN is critically involved in virtually all pathways of gene expression, ranging from transcription to RNA silencing. Owing to its high protein-protein binding affinity coexistent with enzymatic activity, TSN can exert its biochemical function by acting as both a scaffolding molecule of large multiprotein complexes and/or as a nuclease. TSN is indispensible for normal development and stress resistance, whereas its increased expression is closely associated with various types of cancer. Thus, TSN is an attractive target for anti-cancer therapy and a potent tumor marker. Considering ever increasing interest to further understand a multitude of TSN-mediated processes and a mechanistic role of TSN in these processes, here we took an attempt to summarize and update the available information about this intriguing multifunctional protein.

PMID:
27612014
PMCID:
PMC5071578
DOI:
10.1038/cdd.2016.93
[Indexed for MEDLINE]
Free PMC Article

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