%0 Electronic Article %A Han, Yanping and Chen, Dong and Yan, Yanfeng and Gao, Xiaofang and Liu, Zizhong and Xue, Yaqiang and Zhang, Yi and Yang, Ruifu %I American Society for Microbiology %D 2019 %D 2019 %G English %@ 2379-5077 %~ Hochschule Zittau / Görlitz, Hochschulbibliothek %T Hfq Globally Binds and Destabilizes sRNAs and mRNAs in Yersinia pestis %V 4 %J mSystems %V 4 %N 4 %U http://dx.doi.org/10.1128/msystems.00245-19 %X Discovered in 1968 as an Escherichia coli host factor that was essential for replication of the bacteriophage Qβ, the Hfq protein is a ubiquitous and highly abundant RNA-binding protein in many bacteria. With the assistance of Hfq, small RNAs in bacteria play important roles in regulating the stability and translation of mRNAs by base pairing. In this study, we want to elucidate the Hfq-assisted sRNA-mRNA regulation in Yersinia pestis . A global map of Hfq interaction sites in Y. pestis was obtained by sequencing cDNAs converted from the Hfq-bound RNA fragments using UV cross-linking coupled immunoprecipitation technology. We demonstrate that Hfq could bind to hundreds of sRNAs and the majority of mRNAs in Y. pestis . The enriched binding motifs in sRNAs and mRNAs are complementary to each other, suggesting a general base-pairing mechanism for sRNA-mRNA interaction. The Hfq-bound sRNA and mRNA regions were both destabilized. The results suggest that Hfq binding facilitates sRNA-mRNA base pairing and coordinates their degradation, which might enable Hfq to surveil the homeostasis of most mRNAs in bacteria. %Z https://katalog.hszg.de/Record/ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9tc3lzdGVtcy4wMDI0NS0xOQ %U https://katalog.hszg.de/Record/ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9tc3lzdGVtcy4wMDI0NS0xOQ