Sep 7, 2006 · RNase II is a ubiquitous exoribonuclease that processively hydrolyses RNA in the 3′ to 5′ direction, releasing 5′ monophosphates 1. The enzyme binds RNA and in the presence of divalent...

Jul 5, 2006 · We propose a reaction mechanism for exonucleolytic RNA degradation involving key conserved residues. Our three-dimensional model corroborates all existing biochemical data for RNase II, and elucidates the general basis for RNA degradation. Moreover, it reveals important structural features that can be extrapolated to other members of this family.

Dec 25, 2024 · RNASE2 (Ribonuclease A Family Member 2) is a Protein Coding gene. Diseases associated with RNASE2 include Pulmonary Eosinophilia and Esophagitis. Among its related pathways is Innate Immune System. Gene Ontology (GO) annotations related to this gene include nucleic acid binding and RNA nuclease activity. An important paralog of this gene is RNASE3.

RNase II is a ubiquitous enzyme that degrades single-stranded RNAs processively in the 3′-to5′-direction, resulting in the generation of 5′-mononucleotides. Ten nucleotides is the minimum length of the RNA molecule needed to detect activity in RNase II, and the end product of degradation of this enzyme is a 4-nucleotide RNA oligomer (13–15).

RNase II is the most active exoribonuclease in Escherichia coli cell extracts. Yet, its removal appears to have no deleterious effect on growing cells. Here, we show that RNase II is required for cell survival during prolonged stationary phase and upon starvation.

One of these, RNase II, a monomer with a molecular mass of 72.5 kDa, is hydrolytic and accounts for up to 90% of the exoribonucleolytic activity in crude extracts . The other, polynucleotide phosphorylase (PNPase), a trimer with 78-kDa subunits, is phosphorolytic and accounts for the remaining 10% of the exoribonuclease activity in E. coli ...

Feb 14, 2020 · Enzymatic analysis revealed that Alr1240 is an exoribonuclease II (RNase II), as it only degrades non-structured single-stranded RNA substrates. In contrast to known RNase E-interacting ribonucleases, which bind to the noncatalytic domain of RNase E, the Anabaena RNase II was shown to associate with the catalytic domain of RNase E.

Sep 1, 2006 · In a recent issue of Nature, Frazão et al. 1 report the X-ray crystallographic structure of the 3′→5′ exoribonuclease RNase II from E. coli. 3′ exoribonucleases act on many different RNA species...

Here we review recent progresses in the understanding of the degradation mechanism of RNase II, based on mutational analysis and their characterization regarding catalysis and RNA affinity.

Apr 17, 2020 · Enzymatic analysis revealed that Alr1240 is an exoribonuclease II (RNase II), as it only degrades non-structured single-stranded RNA substrates. In contrast to known RNase E-interacting ribonucleases, which bind to the noncatalytic domain of RNase E, the Anabaena RNase II was shown to associate with the catalytic domain of RNase E.