%0 Journal Article %1 chao_vivo_2017 %A Chao, Yanjie %A Li, Lei %A Girodat, Dylan %A Förstner, Konrad U. %A Said, Nelly %A Corcoran, Colin %A Śmiga, Michał %A Papenfort, Kai %A Reinhardt, Richard %A Wieden, Hans-Joachim %A Luisi, Ben F. %A Vogel, Jörg %D 2017 %J Molecular Cell %K 3′_UTR ArcZ Hfq RNA_degradome RNase_E RprA TIER-seq non-coding_RNA sRNA_maturation uridine_ruler %N 1 %P 39--51 %R 10.1016/j.molcel.2016.11.002 %T In Vivo Cleavage Map Illuminates the Central Role of RNase E in Coding and Non-coding RNA Pathways %U http://www.sciencedirect.com/science/article/pii/S1097276516307109 %V 65 %X Summary Understanding RNA processing and turnover requires knowledge of cleavages by major endoribonucleases within a living cell. We have employed TIER-seq (transiently inactivating an endoribonuclease followed by RNA-seq) to profile cleavage products of the essential endoribonuclease RNase E in Salmonella enterica. A dominating cleavage signature is the location of a uridine two nucleotides downstream in a single-stranded segment, which we rationalize structurally as a key recognition determinant that may favor RNase E catalysis. Our results suggest a prominent biogenesis pathway for bacterial regulatory small RNAs whereby RNase E acts together with the RNA chaperone Hfq to liberate stable 3′ fragments from various precursor RNAs. Recapitulating this process in vitro, Hfq guides RNase E cleavage of a representative small-RNA precursor for interaction with a mRNA target. In vivo, the processing is required for target regulation. Our findings reveal a general maturation mechanism for a major class of post-transcriptional regulators.

@article{chao_vivo_2017, abstract = {Summary Understanding RNA processing and turnover requires knowledge of cleavages by major endoribonucleases within a living cell. We have employed TIER-seq (transiently inactivating an endoribonuclease followed by RNA-seq) to profile cleavage products of the essential endoribonuclease RNase E in Salmonella enterica. A dominating cleavage signature is the location of a uridine two nucleotides downstream in a single-stranded segment, which we rationalize structurally as a key recognition determinant that may favor RNase E catalysis. Our results suggest a prominent biogenesis pathway for bacterial regulatory small RNAs whereby RNase E acts together with the RNA chaperone Hfq to liberate stable 3′ fragments from various precursor RNAs. Recapitulating this process in vitro, Hfq guides RNase E cleavage of a representative small-RNA precursor for interaction with a mRNA target. In vivo, the processing is required for target regulation. Our findings reveal a general maturation mechanism for a major class of post-transcriptional regulators.}, added-at = {2019-10-23T15:12:39.000+0200}, author = {Chao, Yanjie and Li, Lei and Girodat, Dylan and Förstner, Konrad U. and Said, Nelly and Corcoran, Colin and Śmiga, Michał and Papenfort, Kai and Reinhardt, Richard and Wieden, Hans-Joachim and Luisi, Ben F. and Vogel, Jörg}, biburl = {https://www.bibsonomy.org/bibtex/2d68ad3fc88864ca3f0312cee0ed885cf/cusysmed}, doi = {10.1016/j.molcel.2016.11.002}, interhash = {e5ebe41cc3fa65eab558beb1e0107acc}, intrahash = {d68ad3fc88864ca3f0312cee0ed885cf}, issn = {1097-2765}, journal = {Molecular Cell}, keywords = {3′_UTR ArcZ Hfq RNA_degradome RNase_E RprA TIER-seq non-coding_RNA sRNA_maturation uridine_ruler}, month = jan, number = 1, pages = {39--51}, timestamp = {2019-10-23T15:12:39.000+0200}, title = {In {Vivo} {Cleavage} {Map} {Illuminates} the {Central} {Role} of {RNase} {E} in {Coding} and {Non}-coding {RNA} {Pathways}}, url = {http://www.sciencedirect.com/science/article/pii/S1097276516307109}, urldate = {2018-06-22}, volume = 65, year = 2017 }