Article abstract
Nature Structural & Molecular Biology 15, 206 - 212 (2008)
Published online: 20 January 2008 | doi:10.1038/nsmb.1376
Structural insights into the dual activity of RNase J
Inés Li de la Sierra-Gallay1, Léna Zig2, Ailar Jamalli2 & Harald Putzer2
Abstract
The maturation and stability of RNA transcripts is controlled by a combination of endo- and exoRNases. RNase J is unique, as it combines an RNase E–like endoribonucleolytic and a 5'-to-3' exoribonucleolytic activity in a single polypeptide. The structural basis for this dual activity is unknown. Here we report the crystal structures of Thermus thermophilus RNase J and its complex with uridine 5'-monophosphate. A binding pocket coordinating the phosphate and base moieties of the nucleotide in the vicinity of the catalytic center provide a rationale for the 5'-monophosphate–dependent 5'-to-3' exoribonucleolytic activity. We show that this dependence is strict; an initial 5'-PPP transcript cannot be degraded exonucleolytically from the 5'-end. Our results suggest that RNase J might switch promptly from endo- to exonucleolytic mode on the same RNA, a property that has important implications for RNA metabolism in numerous prokaryotic organisms and plant organelles containing RNase J orthologs.
- FRC550, Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France.
- Université Paris 7-Denis Diderot, CNRS UPR9073, Institut de Biology Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France.
Correspondence to: Harald Putzer2 e-mail: putzer@ibpc.fr
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