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.

RNase II, the 644 amino-acid product of the rnb gene, is the major hydrolytic exoribonuclease in E. coli. RNase II acts processively from the 3′ end of single-stranded RNA substrates and accounts for approximately 90% of the total exoribonucleolytic activity in cell extracts [6,11].

2006年9月7日 · 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...

2006年7月5日 · Ribonuclease II (RNase II) is a major exoribonuclease that intervenes in all of these fundamental processes; it can act independently or as a component of the exosome, an essential RNA-degrading multiprotein complex.

Here, we show that the 3′→5′ exonuclease RNase II plays an important role in RelE-independent A-site cleavage. Instead of A-site cleavage, translational pausing in ΔRNase II cells produces transcripts that are truncated +12 and +28 nucleotides downstream of the A-site codon.

2020年4月17日 · To our knowledge, Anabaena RNase II is an unusual ribonuclease that interacts with the catalytic domain of RNase E, and it may represent a new type of RNA degradosome and a novel mechanism for regulating the activity of the RNA degradosome.

We have assessed the ability of small RNA substrates containing defined stem-loop structures and variable 3′ extensions to impede the exonucleolytic activity of these enzymes.

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.

RNase II is a key exoribonuclease involved in the maturation, turnover, and quality control of RNA. RNase II homologues are components of the exosome, a complex of exoribonucleases. The structure of RNase II unraveled crucial aspects of the mechanism of RNA degradation.

RNase II is the most active exoribonuclease in extracts of E. coli, accounting for 95–98% of hydrolytic activity when poly (A) is used as the substrate (Cheng et al. 1998). Because it is such an active enzyme, RNase II was one of the first RNases to be identified and purified .