Abstract
Correction: Functional Role of Glutamine 28 and Arginine 39 in Double Stranded RNA Cleavage by Human Pancreatic Ribonuclease
Highlights
Human pancreatic ribonuclease (HPR) is a member of an ancient superfamily of proteins, called RNase A superfamily [1]
HPR exhibits a remarkably high activity against double stranded RNA. This high dsRNA cleavage activity of HPR suggests the enzyme to be playing a role in host defense
In this study we have investigated the role of glutamine 28, glycine and arginine in the dsRNA cleavage activity of HPR
Summary
Human pancreatic ribonuclease (HPR) is a member of an ancient superfamily of proteins, called RNase A superfamily [1]. Unlike the other members of the family, HPR displays substantial activity on double stranded (ds) RNA even under conditions in which dsRNA maintains stable secondary structure [2]. This activity is unrelated to digestion and is thought to be involved in the host-defense against pathogenic viruses [2,3]. The members of RNase A superfamily cleave single stranded (ss) RNA by a transesterification reaction, which requires linear arrangement of the 29oxygen atom, 59oxygen atom and the intermediate phosphorus atom [8] This ‘inline’ orientation of phosphodiester bond is not possible in dsRNA, which adopts helical secondary structure [9]. We have reported that lysine 6, arginine 32, lysine 62 and lysine 74 do not play a direct role in the dsRNA cleavage activity of HPR, lysine 6, lysine 74 and lysine 62 appear to be involved in general catalysis, structural integrity and stability and DNA helix unwinding activity of HPR [12]
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