Regular ArticleStructural Modifications of RNA Influence the 5′ Exoribonucleolytic Hydrolysis by XRN1 and HKE1 ofSaccharomyces cerevisiae☆
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Subgenomic flaviviral RNAs: What do we know after the first decade of research
2018, Antiviral ResearchCitation Excerpt :XRN-1 is a highly processive enzyme that has an RNA-helicase activity and is generally capable of digesting structured RNAs. When the ability of SLII, SLIV and DBI of WNV 3′UTR to stall XRN-1 was discovered, only the homopolymer G stretches of 9 + nucleotides were known to efficiently halt RNA digestion by XRN-1, whereas stem loops were thought to have very little effect on processivity of 5’ -> 3′ exoribonucleases (Poole and Stevens, 1997). It was therefore puzzling why stem loops within the faviviral genomes have such a dramatic effect on XRN-1 processing and at the same time do not interfere with viral polymerase moving in 3′ to 5′ direction on the viral template (+) RNA strand while synthesising (−) RNA strand.
Cellular 5′-3′ mRNA exonuclease Xrn1 controls double-stranded RNA accumulation and anti-viral responses
2015, Cell Host and MicrobeCitation Excerpt :The impressive increase in dsRNA accumulation in Xrn1-depleted, VacV-infected cells was unforeseen, as Xrn1 is a processive exonuclease whose substrate is single-stranded mRNA with exposed 5′-phosphate termini. Previous studies, however, have shown that it is capable of processing RNA stem loops (Decker and Parker, 1993; Poole and Stevens, 1997) and RNA:DNA duplexes (Jinek et al., 2011) provided that the 5′ RNA overhang is of sufficient length. Therefore Xrn1 may function not only to control VacV mRNA turnover, but also destabilize RNA duplexes and directly degrade imperfectly annealed strands.
Coupled 5' Nucleotide Recognition and Processivity in Xrn1-Mediated mRNA Decay
2011, Molecular CellRrp17p Is a Eukaryotic Exonuclease Required for 5′ End Processing of Pre-60S Ribosomal RNA
2009, Molecular CellCitation Excerpt :Significant differences in the efficiency of degradation between 5′-monophosphorylated and triphosphorylated substrate (Figures 4C, S5A, and S5B) were observed, indicating that Rrp17p is indeed sensitive to the phosphorylation state of the 5′ end. We performed a similar analysis with substrates carrying a 5′-hydroxyl group or a 5′mG-cap structure, features known to inhibit Rat1p and Xrn1p activity (Poole and Stevens, 1997). However, while the 5′mG-cap containing substrate was less efficiently degraded than the control 5′ or 3′ end-labeled substrates, the 5′-hydroxyl end substrate was not (Figures 4C, S5C, and S5D); it therefore appears that Rrp17p has a somewhat different mode of function to Rat1p and Xrn1p.
Rat1p nuclease
2001, Methods in EnzymologyCitation Excerpt :Xrn2 is also inhibited by the presence of strong secondary structures within RNAs. Oligo(G) tracts of 16 to 18 nucleotides in length effectively block degradation by Xrn2.15 RNAs containing such oligo(G) tracts are degraded from the 5′ end up to the 5′ side of the oligo(G) tract; the remaining 3′ fragment is resistant to further digestion.
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XRN1, protein encoded by theXRN1gene ofS. cerevisiae;HKE1, protein encoded by theHKE1gene ofS. cerevisiae;PABP, poly(A) binding protein
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