A novel mechanism of RNase L inhibition: Theiler\u27s virus L* protein prevents 2-5A from binding to RNase L [PDF]
The OAS/RNase L pathway is one of the best-characterized effector pathways of the IFN antiviral response. It inhibits the replication of many viruses and ultimately promotes apoptosis of infected cells, contributing to the control of virus spread ...
Drappier, Melissa+8 more
core +4 more sources
Zebrafish RNase T2 genes and the evolution of secretory ribonucleases in animals
Background Members of the Ribonuclease (RNase) T2 family are common models for enzymological studies, and their evolution has been well characterized in plants.
Essner Jeffrey J+5 more
doaj +1 more source
Inhibition of Murine Cytomegalovirus Infection in Animals by RNase P-Associated External Guide Sequences. [PDF]
External guide sequence (EGS) RNAs are associated with ribonuclease P (RNase P), a tRNA processing enzyme, and represent promising agents for gene-targeting applications as they can direct RNase-P-mediated cleavage of a target mRNA.
Li, Wei+9 more
core +2 more sources
RNase P Branches Out from RNP to Protein: Organelle-Triggered Diversification? [PDF]
RNase P is the enzyme that removes 5′ leader sequences from precursor tRNAs. Remarkably, in most organisms, RNase P is a ribonucleoprotein particle where the RNA component is responsible for catalysis. In this issue of Genes \u26 Development, Gutmann and
Borah, Sumit+2 more
core +3 more sources
Protein synthesis inhibitors and catalytic RNA Effect of puromycin on tRNA precursor processing by the RNA component of Escherichia coli RNase P [PDF]
RNase P and ribosomes must interact with similar substrate molecules, tRNA precursors in the case of RNase P and aminoacyl-, peptidyl- or free tRNAs in the case of ribosomes.
Direcció Tècnica d'Urbanisme+1 more
core +1 more source
Influence of Conformation of M. tuberculosis RNase P Protein Subunit on Its Function. [PDF]
RNase P is an essential enzyme that processes 5' end leader sequence of pre-tRNA to generate mature tRNA. The bacterial RNase Ps contain a RNA subunit and one protein subunit, where the RNA subunit contains the catalytic activity.
Alla Singh+3 more
doaj +1 more source
Architecture and Function of the Human Endonucleases RNase P and RNase MRP [PDF]
AbstractIn the past decade, important advances have been made in our knowledge of the composition of human RNase MRP and RNase P complexes. Both ribonucleoprotein particles function as endonucleases and contain RNA components that are structurally related.
Eenennaam, H. van+3 more
openaire +4 more sources
Insights into the structure and activity of prototype foamy virus RNase H
Background RNase H is an endonuclease that hydrolyzes the RNA strand in RNA/DNA hybrids. Retroviral reverse transcriptases harbor a C-terminal RNase H domain whose activity is essential for viral replication.
Leo Berit+4 more
doaj +1 more source
Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP
Ribozyme-based RNase MRP is an essential eukaryotic enzyme involved in the maturation of rRNA and is evolutionarily related to RNase P. Here, the authors present the 3.0 Å cryo-EM structure of the S.
Anna Perederina+6 more
doaj +1 more source
Identity of the RNase MRP– and RNase P–associated Th/To autoantigen [PDF]
AbstractObjectiveTo characterize the molecular identity of the Th/To autoantigen, which is targeted by autoantibodies in scleroderma and which is associated with the human RNase MRP and RNase P ribonucleoprotein complexes.MethodsProteins immunoprecipitated by anti‐Th/To+ patient antisera from biotinylated total HeLa cell extracts were analyzed by ...
Eenennaam, H. van+5 more
openaire +4 more sources