Chapter 26: Q2P (page 979)
The bacterial enzyme polynucleotide phosphorylase (PNPase) is a exoribonuclease that degrades mRNA. (a) The enzyme catalyzes a phosphorolysis reaction, as does glycogen phosphorylase (Section ), rather than hydrolysis. Write an equation for the mRNA phosphorolysis reaction. (b) In vitro, PNPase also catalyzes the reverse of the phosphorolysis reaction. What does this reaction accomplish and how does it differ from the reaction carried out by RNA polymerase? (c) PNPase includes a binding site for long ribonucleotides, which may promote the enzyme's processivity. Why would this be an advantage for the primary activity of PNPase in vivo?
Short Answer
- The reverse reaction of PNPase synthesizes polyribonucleotides. PNPase differs from RNA polymerase as it does not require a template.
- In the cell, PNPase degrades mRNAs to nucleoside diphosphates which will be increased by the binding of large ribonucleotides.