Maturation of Polycistronic mRNAs by the Endoribonuclease RNase Y and Its Associated Y-Complex in Bacillus Subtilis
Author(s)
Losick, Richard; DeLoughery, Aaron; Lalanne, Jean-Benoit; Li, Gene-Wei
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Endonucleolytic cleavage within polycistronic mRNAs can lead to differential stability, and thus discordant abundance, among cotranscribed genes. RNase Y, the major endonuclease for mRNA decay in Bacillus subtilis, was originally identified for its cleavage activity toward the cggR-gapA operon, an event that differentiates the synthesis of a glycolytic enzyme from its transcriptional regulator. A three-protein Y-complex (YlbF, YmcA, and YaaT) was recently identified as also being required for this cleavage in vivo, raising the possibility that it is an accessory factor acting to regulate RNase Y. However, whether the Y-complex is broadly required for RNase Y activity is unknown. Here, we used end-enrichment RNA sequencing (Rend-seq) to globally identify operon mRNAs that undergo maturation posttranscriptionally by RNase Y and the Y-complex. We found that the Y-complex is required for the majority of RNase Y-mediated mRNA maturation events and also affects riboswitch abundance in B. subtilis. In contrast, noncoding RNA maturation by RNase Y often does not require the Y-complex. Furthermore, deletion of RNase Y has more pleiotropic effects on the transcriptome and cell growth than deletions of the Y-complex. We propose that the Y-complex is a specificity factor for RNase Y, with evidence that its role is conserved in Staphylococcus aureus.
Date issued
2018-06Department
Massachusetts Institute of Technology. Department of Biology; Massachusetts Institute of Technology. Department of PhysicsJournal
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences (U.S.)
Citation
DeLoughery, Aaron et al. “Maturation of Polycistronic mRNAs by the Endoribonuclease RNase Y and Its Associated Y-Complex in Bacillus Subtilis.” Proceedings of the National Academy of Sciences 115, 24 (May 2018): E5585–E5594 © 2018 National Academy of Sciences
Version: Final published version
ISSN
0027-8424
1091-6490