Stress Responsive Zinc-finger Protein Gene of Populus euphratica in Tobacco Enhances Salt Tolerance

The Populus euphratica stress responsive zinc-finger protein gene PSTZ, which encodes a protein including typical Cys2/His2 zinc finger structure, was isolated by reverse transcription-polymerase chain reaction from P. euphratica. Northern hybridization revealed that its expression was induced under drought and salt stress conditions. To examine its function, cDNA of the PSTZ gene, driven by the cauliflower mosaic virus 35S promoter, was cloned into a plant expression vector pBin438 and introduced into tobacco plants. Transgenic tobacco showed an enhanced salt tolerance, suggesting that PSTZ may play a role in plant responsiveness to salt stress.

Expression and function of long non-coding RNA DLX6-AS1 in endometrial cancer

Background:LncRNA DLX6-AS1 has been uncovered to exert effects on various cancers.Nevertheless,the impacts of DLX6-AS1 on endometrial cancer(EC)development remained obscure.The study explored the influence of DLX6-AS1 on EC progression via the microRNA(miR)-374a-3p/zinc-finger protein(ZFX)axis.Methods:EC cell lines were collected and DLX6-AS1,miR-374a-3p,and ZFX levels in EC cell lines were detected.The EC cells were transfected with DLX6-AS1,miR-374a-3p,and ZFX constructs to examine the biological functions of EC cells.The xenograft model was established for detecting tumor growth.Rescue experiments were conducted to verify the interaction of DLX6-AS1,miR-374a-3p,and ZFX in EC cells.Results:DLX6-AS1 and ZFX levels were elevated,while miR-374a-3p exhibited a reduced level in EC cells.Silencing DLX6-AS1 and elevated miR-374a-3p expressions repressed the biological activities of EC cells.Reduced DLX6-AS1 repressed tumor development.MiR-374a-3p silencing reversed the impacts of DLX6-AS1 silencing,while ZFX overexpression abrogated the impacts of miR-374a-3p elevation on EC cell growth.Mechanically,DLX6-AS1 was found to bind to miR-374a-3p,and miR-374a-3p targeted ZFX.Conclusion:DLX6-AS1 depletion restricts the malignant phenotype of EC cells.The study might provide novel therapeutic biomarkers for EC treatment.

DEXH-Box protein DHX30 is required for optimal function of the zinc-finger antiviral protein

The zinc-finger antiviral protein(ZAP)is a host factor that specifically inhibits the replication of certain viruses by eliminating viral mRNAs in the cytoplasm.In previous studies,we demonstrated that ZAP directly binds to the viral mRNAs and recruits the RNA exosome to degrade the target RNA.In this article,we provide evidence that a DEXH box RNA helicase,DHX30,is required for optimal antiviral activity of ZAP.Pull-down and co-immunoprecipitation assays demonstrated that DHX30 and ZAP interacted with each other via their N terminal domains.Downregulation of DHX30 with shRNAs reduced ZAP’s antiviral activity.These data implicate that DHX30 is a cellular factor involved in the antiviral function of ZAP.

Analyses of SELEX-derived ZAP-binding RNA aptamers suggest that the binding specificity is determined by both structure and sequence of the RNA

The zinc-finger antiviral protein(ZAP)is a host factor that specifically inhibits the replication of certain viruses,including murine leukemia virus,Sindbis virus and Ebola virus,by targeting the viral mRNAs for degradation.ZAP directly binds to the target viral mRNA and recruits the cellular RNA degradation machinery to degrade the RNA.No significant sequence similarity or obvious common motifs have been found in the so far identified target viral mRNAs.The minimum length of the target sequence is about 500 nt long.Short workable ZAP-binding RNAs should facilitate further studies on the ZAP-RNA interaction and characterization of such RNAs may provide some insights into the underlying mechanism.In this study,we used the SELEX method to isolate ZAP-binding RNA aptamers.After 21 rounds of selection,ZAP-binding aptamers were isolated.Sequence analysis revealed that they are G-rich RNAs with predicted stem-loop structures containing conserved“GGGUGG”and“GAGGG”motifs in the loop region.Insertion of the aptamer sequence into a luciferase reporter failed to render the reporter sensitive to ZAP.However,overexpression of the aptamers modestly but significantly reduced ZAP’s antiviral activity.Substitution of the conserved motifs of the aptamers significantly impaired their ZAP-binding ability and ZAP-antagonizing activity,suggesting that the RNA sequence is important for specific interaction between ZAP and the target RNA.The aptamers identified in this report should provide useful tools to further investigate the details of the interaction between ZAP and the target RNAs.