Tudor Staphylococcal Nuclease plays two antagonistic roles in RNA metabolism under stress

Gutiérrez-Beltrán, Emilio; Bozhkov, Peter V.; Moschou, Panagiotis N.

doi:10.1080/15592324.2015.1071005

Cited by 9 publications

(8 citation statements)

References 29 publications

(36 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One of the most enriched categories of SG‐associated proteins is RBPs regulating RNA transport, silencing, translation and degradation (Wolozin & Apicco, 2015 ). Likewise, RBPs accounted for 55% of TSN2_HS and TSN2_NS interactomes (Fig 1F ), providing a further mechanistic explanation for the previously established role of TSN in mRNA stabilization and degradation (Gutierrez‐Beltran et al , 2015a ).…”

Section: Discussionsupporting

confidence: 73%

“…TSN is known to be critically involved in the regulation of virtually all pathways of gene expression, ranging from transcription to RNA silencing (Gutierrez‐Beltran et al , 2016 ; Chou et al , 2017 ). For example, Arabidopsis TSN1 and TSN2, two functionally redundant TSN homologues, have been described to play two antagonistic roles in RNA metabolism during stress (Gutierrez‐Beltran et al , 2015a ). Yet, the cellular level of TSN protein itself should be carefully regulated.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Tudor staphylococcal nuclease is a docking platform for stress granule components and is essential for SnRK1 activation in Arabidopsis

et al. 2021

Self Cite

View full text Add to dashboard Cite

Tudor staphylococcal nuclease (TSN; also known as Tudor‐SN, p100, or SND1) is a multifunctional, evolutionarily conserved regulator of gene expression, exhibiting cytoprotective activity in animals and plants and oncogenic activity in mammals. During stress, TSN stably associates with stress granules (SGs), in a poorly understood process. Here, we show that in the model plant Arabidopsis thaliana, TSN is an intrinsically disordered protein (IDP) acting as a scaffold for a large pool of other IDPs, enriched for conserved stress granule components as well as novel or plant‐specific SG‐localized proteins. While approximately 30% of TSN interactors are recruited to stress granules de novo upon stress perception, 70% form a protein–protein interaction network present before the onset of stress. Finally, we demonstrate that TSN and stress granule formation promote heat‐induced activation of the evolutionarily conserved energy‐sensing SNF1‐related protein kinase 1 (SnRK1), the plant orthologue of mammalian AMP‐activated protein kinase (AMPK). Our results establish TSN as a docking platform for stress granule proteins, with an important role in stress signalling.

show abstract

Section: Discussionsupporting

confidence: 73%

Section: Introductionmentioning

confidence: 99%

Tudor staphylococcal nuclease is a docking platform for stress granule components and is essential for SnRK1 activation in Arabidopsis

et al. 2021

Self Cite

View full text Add to dashboard Cite

show abstract

“…We assumed that SFH8 clusters have increased liquidity and reduced stability at the PM, compared to filaments, as they showed features of LLPS which could imply a rapid exchange of SFH8 molecules with the cytoplasm. Although FRAP is not a decisive feature for testing LLPS, liquid-like clusters can display rapid internal reorganization and a corresponding rapid fluorescent recovery on the order of seconds, whereas more solid-like condensates such as non-dynamic filaments may show little recovery (Gutierrez-Beltran et al, 2015). FRAP showed that SFH8-mNeon was highly dynamic at the PM close to the meristem, unlike the distal meristem in which SFH8 lacked dynamicity ( Figure 3G ).…”

Section: Resultsmentioning

confidence: 99%

Phase transitions of a SEC14-like condensate at Arabidopsis plasma membranes regulate root growth

Liu

Mentzelopoulou

Deli

et al. 2022

Preprint

View full text Add to dashboard Cite

Robust development can be modulated by local protein accumulation which is sometimes manifested as polarity patterns; yet, the mechanisms that lead to these patterns are largely unknown. Using the model plant Arabidopsis, we report that auxin-induced polar patterns can be reinforced by the phase transition of a SEC14-like lipid-binding protein at the plasma membrane. Using imaging, genetics, and in vitro reconstitutions, we show that the SEC14-like phase transition is promoted outside the stem cell root niche through its association with the caspase-like protease separase and conserved microtubule motors in a plasma membrane interface. Separase cleaves SEC14-like to promote its transition from liquid-like clusters to solid-like filaments. Filaments self-amplify and potentiate the robustness and maintenance of plasma membrane domains through associations with polar proteins. This work uncovers that robust cell patterns involve proteolysis-mediated phase transitions at unpreceded plasma membrane interfaces.

show abstract

“…In Arabidopsis, the two homologous, redundant Tudor-SN forms have been shown to be required in promoting cell viability and abiotic stress tolerance (dit Frey et al, 2010; Liu et al, 2010b) and are components of both stress granules and P-bodies (Gutierrez-Beltran et al, 2015b). Its role in stress tolerance is attributed to its capacity to stabilize mRNAs involved in stress-related pathways (Gutiérrez-Beltran et al, 2015a, 2015b.…”

Section: Discussionmentioning

confidence: 99%

Multifunctional RNA Binding Protein OsTudor-SN in Storage Protein mRNA Transport and Localization

et al. 2017

View full text Add to dashboard Cite

The multifunctional RNA-binding protein Tudor-SN plays multiple roles in transcriptional and posttranscriptional processes due to its modular domain structure, consisting of four tandem Staphylococcus nuclease (SN)-like domains (4SN), followed by a carboxyl-terminal Tudor domain, followed by a fifth partial SN sequence (Tsn). In plants, it confers stress tolerance, is a component of stress granules and P-bodies, and may participate in stabilizing and localizing RNAs to specific subdomains of the cortical-endoplasmic reticulum in developing rice (Oryza sativa) endosperm. Here, we show that, in addition to the intact rice OsTudor-SN protein, the 4SN and Tsn modules exist as independent polypeptides, which collectively may coassemble to form a complex population of homodimer and heteroduplex species. The 4SN and Tsn modules exhibit different roles in RNA binding and as a protein scaffold for stress-associated proteins and RNA-binding proteins. Despite their distinct individual properties, mutations in both the 4SN and Tsn modules mislocalize storage protein mRNAs to the cortical endoplasmic reticulum. These results indicate that the two modular peptide regions of OsTudor-SN confer different cellular properties but cooperate in mRNA localization, a process linking its multiple functions in the nucleus and cytoplasm.mRNA localization is readily evident in structurally polarized somatic cells

show abstract

Tudor Staphylococcal Nuclease plays two antagonistic roles in RNA metabolism under stress

Cited by 9 publications

References 29 publications

Tudor staphylococcal nuclease is a docking platform for stress granule components and is essential for SnRK1 activation in Arabidopsis

Tudor staphylococcal nuclease is a docking platform for stress granule components and is essential for SnRK1 activation in Arabidopsis

Phase transitions of a SEC14-like condensate at Arabidopsis plasma membranes regulate root growth

Multifunctional RNA Binding Protein OsTudor-SN in Storage Protein mRNA Transport and Localization

Contact Info

Product

Resources

About