RRC ID 53764
著者 Bandyra KJ, Sinha D, Syrjanen J, Luisi BF, De Lay NR.
タイトル The ribonuclease polynucleotide phosphorylase can interact with small regulatory RNAs in both protective and degradative modes.
ジャーナル RNA
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 against the destructive activity of the ribonuclease. In vitro, PNPase, Hfq, and sRNA can form a ternary complex in which the ribonuclease plays a nondestructive, structural role. Such ternary complexes might be formed transiently in vivo, but could help to stabilize particular sRNAs and remodel their population on Hfq. Taken together, our results indicate that PNPase can be programmed to act on RNA in either destructive or stabilizing modes in vivo and may form complex, protective ribonucleoprotein assemblies that shape the landscape of sRNAs available for action.
巻・号 22(3)
ページ 360-72
公開日 2016-3-1
DOI 10.1261/rna.052886.115
PII rna.052886.115
PMID 26759452
PMC PMC4748814
MeSH Hydrolysis Polyribonucleotide Nucleotidyltransferase / metabolism* Protein Binding RNA / metabolism*
IF 4.32
引用数 29
リソース情報
原核生物(大腸菌)