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.
Highlights
TSN is an evolutionarily conserved protein having a pivotal role in the regulation of gene expression
TSN acts both as a scaffolding protein and as a nuclease
How is nucleolytic activity of TSN regulated in vivo and how this affects interaction of TSN with downstream targets?
Summary
B. mori X. laevis Human cells D. melanogaster Human cells Arabidopsis Human cells. B. mori Arabidopsis c-Myb and Pim-1 STAT6 and CBP STAT6 and RHA STAT6 and PC1 STAT5 EBNA2 and TFIIE PPARγ. Prp[8] SmB, SmD1 and SmD3 SAM68 SmD1 Ago[2], FMRP, VIG and FXR AEG-1 Ago[1] and Ago[2] Ago[1] and Ago[2]
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