A new RNase activity, tentatively named RNase V, was found in cell-free extracts of E. coli. This activity requires ribosomes, G and T factors, tRNA, K + or NH 4 + , Mg 2+ , GTP, and a sulfhydryl compound to degrade poly U, poly A, T4 phage mRNA, or E. coli mRNA.

Ribonuclease V (EC 3.1.27.8, endoribonuclease V) is an enzyme. [1] This enzyme catalyses the following chemical reaction Hydrolysis of poly(A), forming oligoribonucleotides and ultimately 3'-AMP

Ribonuclease (commonly abbreviated RNase) is a type of nuclease that catalyzes the degradation of RNA into smaller components. Ribonucleases can be divided into endoribonucleases and exoribonucleases, and comprise several sub-classes within the EC 2.7 (for the phosphorolytic enzymes) and 3.1 (for the hydrolytic enzymes) classes of enzymes.

Aug 20, 1971 · The relationship between RNase II and RNase V activities in Escherichia coli was investigated. The experiments suggest the possibility that the activity named RNase V was due to residual RNase II activity or a related enzyme on ribosomes.

Ribonuclease V1 (RNase V1) is a ribonuclease enzyme found in the venom of the Caspian cobra (Naja oxiana). [1] It cleaves double-stranded RNA in a non-sequence-specific manner, usually requiring a substrate of at least six stacked nucleotides. [2] Like many ribonucleases, the enzyme requires the presence of magnesium ions for activity. [3]

RNase V1 is an endonuclease that cleaves base-paired nucleotides. RNase V1 is used in rapid analysis of the physical structure of RNA, in combination with single-strand specific RNase A and RNase T1. Source: Manufactured from cobra venom. 30 …

Rnase V1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more

Oct 3, 2015 · Ribonucleases (RNases) that play a key role in RNA metabolism by cleaning the excess of cellular RNA and in maturation of all types of RNA are important catalysts commonly found in nature.

Endonuclease V (EndoV) cleaves the second phosphodiester bond 3′ to a deaminated adenosine (inosine). Although highly conserved, EndoV homologs change substrate preference from DNA in bacteria to RNA in eukaryotes.

1 day ago · The levels of the truncated RNase E-mNeon were elevated in comparison to wild-type RNase E-mNeon, forming occasional large puncta (Fig S12A). The formation of CsrA foci in this strain persists ...