A Tudor staphylococcal nuclease from Penaeus monodon: cDNA cloning and its involvement in RNA interference

Phetrungnapha, Amnat; Panyim, Sakol; Ongvarrasopone, Chalermporn

doi:10.1016/j.fsi.2011.05.026

Cited by 11 publications

(6 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The experiment was based on using dsRNA targeting Tudor-SN (Tudor domain) and Subolesin ( SUB ) to see the effect of Tudor-SN gene knockdown on SUB expression. A similar experimental approach demonstrated the role of Panaeus monodon Tudor-SN in RNAi [ 22 ].…”

Section: Resultsmentioning

confidence: 99%

Nuclease Tudor-SN Is Involved in Tick dsRNA-Mediated RNA Interference and Feeding but Not in Defense against Flaviviral or Anaplasma phagocytophilum Rickettsial Infection

et al. 2015

View full text Add to dashboard Cite

Tudor staphylococcal nuclease (Tudor-SN) and Argonaute (Ago) are conserved components of the basic RNA interference (RNAi) machinery with a variety of functions including immune response and gene regulation. The RNAi machinery has been characterized in tick vectors of human and animal diseases but information is not available on the role of Tudor-SN in tick RNAi and other cellular processes. Our hypothesis is that tick Tudor-SN is part of the RNAi machinery and may be involved in innate immune response and other cellular processes. To address this hypothesis, Ixodes scapularis and I. ricinus ticks and/or cell lines were used to annotate and characterize the role of Tudor-SN in dsRNA-mediated RNAi, immune response to infection with the rickettsia Anaplasma phagocytophilum and the flaviviruses TBEV or LGTV and tick feeding. The results showed that Tudor-SN is conserved in ticks and involved in dsRNA-mediated RNAi and tick feeding but not in defense against infection with the examined viral and rickettsial pathogens. The effect of Tudor-SN gene knockdown on tick feeding could be due to down-regulation of genes that are required for protein processing and blood digestion through a mechanism that may involve selective degradation of dsRNAs enriched in G:U pairs that form as a result of adenosine-to-inosine RNA editing. These results demonstrated that Tudor-SN plays a role in tick RNAi pathway and feeding but no strong evidence for a role in innate immune responses to pathogen infection was found.

show abstract

Section: Resultsmentioning

confidence: 99%

Nuclease Tudor-SN Is Involved in Tick dsRNA-Mediated RNA Interference and Feeding but Not in Defense against Flaviviral or Anaplasma phagocytophilum Rickettsial Infection

et al. 2015

View full text Add to dashboard Cite

show abstract

“…The Tudor-SN protein, also known as p100, SND1, or TSN (Tudor staphylococcal nuclease), shows a certain conservation across different species [3][4][5][6][7][8][9]. In 1995, Tong and colleagues first reported that Tudor-SN serves as a transcriptional coactivator of human Epstein-Barr virus nuclear antigen 2 (EBNA2) and has a molecular weight of approximately 100 kDa (originally termed "p100") [10].…”

Section: Discovery and Preliminary Studymentioning

confidence: 99%

“…In 2003, Caudy et al reported for the first time that the Tudor-SN is a component of the RISC (RNA-induced silencing complex) [46]. Subsequently, there have been several lines of evidence that in multiple species, the Tudor-SN protein can interfere with target mRNA by participating in RISC assembly, but its calcium-dependent nuclease activity is different [9,[46][47][48][49][50][51][52][53][54]. For instance, the Tudor-SN protein in the RISC of Arabidopsis and African trypanosomes possess no or only minor nuclease activity [49][50][51][52]55].…”

Section: Rna Interferencementioning

confidence: 99%

Friend or Foe? The fascinating Tudor-SN protein

et al. 2023

View full text Add to dashboard Cite

Tudor-SN (Tudor staphylococcal nuclease), also known as p100 or SND1 (Staphylococcal nuclease and Tudor domain containing 1), is a structurally conserved protein with diverse functions. Emerging evidence indicates that Tudor-SN plays an essential role in both physiological and pathological processes. Under physiological conditions, Tudor-SN regulates DNA transcription, RNA splicing, RNA stability, RNA interference, and RNA editing, and it is essential for a series of cellular biological events, such as cell cycle progression, cell metabolism, and cell survival, in response to harmful stimuli; thus, Tudor-SN functions as a “friend” to the body. However, Tudor-SN is highly expressed in most tumor cells. As an oncoprotein, Tudor-SN is closely associated with the initiation, development, and metastasis of tumors; thus, Tudor-SN functions as a “foe” to the body. What is the potential mechanism by which Tudor-SN switches from its role as “friend” to its role as “foe”? In this study, we review and summarize the available evidence regarding Tudor-SN protein structure, expression, modification, and mutation to present a novel model of Tudor-SN role switching. This review provides a comprehensive insight into the functional significance of the Tudor-SN protein under physiological and pathological conditions as well as corresponding therapeutic strategies that target Tudor-SN.

show abstract

“…Combination of TRBP with eukaryotic initiation factor 6 leads to an antiviral RNA interference pathway in shrimp Marsupenaeus japonicus [61]. Knockdown of a shrimp tudor staphylococcal nuclease (PmTSN), one of the RISC associated protein involved in post transcriptional regulation, resulted in reduced inhibition of YHV infection mediated by RNAi of YHV in Penaeus monodon [62]. In our studies we found that TAR RNA-binding protein isoform 1 and TSN, both involved in RISC, were down-regulated at 12 hpi.…”

Section: Response Of Immune Related Proteinsmentioning

confidence: 99%

Proteomic analysis by iTRAQ in red claw crayfish, Cherax quadricarinatus, hematopoietic tissue cells post white spot syndrome virus infection

Jeswin

Xie

et al. 2016

Fish & Shellfish Immunology

View full text Add to dashboard Cite

To elucidate proteomic changes of Hpt cells from red claw crayfish, Cherax quadricarinatus, we have carried out isobaric tags for relative and absolute quantitation (iTRAQ) of cellular proteins at both early (1 hpi) and late stage (12 hpi) post white spot syndrome virus (WSSV) infection. Protein database search revealed 594 protein hits by Mascot, in which 17 and 30 proteins were present as differentially expressed proteins at early and late viral infection, respectively. Generally, these differentially expressed proteins include: 1) the metabolic process related proteins in glycolysis and glucogenesis, DNA replication, nucleotide/amino acid/fatty acid metabolism and protein biosynthesis; 2) the signal transduction related proteins like small GTPases, G-protein-alpha stimulatory subunit, proteins bearing PDZ- or 14-3-3-domains that help holding together and organize signaling complexes, casein kinase I and proteins of the MAP-kinase signal transduction pathway; 3) the immune defense related proteins such as α-2 macroglobulin, transglutaminase and trans-activation response RNA-binding protein 1. Taken together, these protein information shed new light on the host cellular response against WSSV infection in a crustacean cell culture.

show abstract

A Tudor staphylococcal nuclease from Penaeus monodon: cDNA cloning and its involvement in RNA interference

Cited by 11 publications

References 41 publications

Nuclease Tudor-SN Is Involved in Tick dsRNA-Mediated RNA Interference and Feeding but Not in Defense against Flaviviral or Anaplasma phagocytophilum Rickettsial Infection

Nuclease Tudor-SN Is Involved in Tick dsRNA-Mediated RNA Interference and Feeding but Not in Defense against Flaviviral or Anaplasma phagocytophilum Rickettsial Infection

Friend or Foe? The fascinating Tudor-SN protein

Proteomic analysis by iTRAQ in red claw crayfish, Cherax quadricarinatus, hematopoietic tissue cells post white spot syndrome virus infection

Contact Info

Product

Resources

About