The ribonuclease polynucleotide phosphorylase can interact with small regulatory RNAs in both protective and degradative modes.

ABSTRACT: In all bacterial species examined thus far, small regulatory RNAs (sRNAs) contribute to intricate patterns of dynamic genetic regulation. Many of the actions of these nucleic acids are mediated by well-characterized chaperones such as the Hfq protein, but genetic screens have also recently identified the 3'-to-5' exoribonuclease polynucleotide phosphorylase (PNPase) as an unexpected stabilizer and facilitator of sRNAs in vivo. To understand how a ribonuclease might mediate these effects, we tested the interactions of PNPase with sRNAs and found that the enzyme can readily degrade these nucleic acids in vitro but, nonetheless, copurifies from cell extracts with the same sRNAs without discernible degradation or modification to their 3' ends, suggesting that the associated RNA is protected ag

SUBMITTER: Bandyra KJ 

PROVIDER: S-EPMC4748814 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature