Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA.

Abstract:

:NanoRNAs are RNA fragments 2 to 5 nucleotides in length that are generated as byproducts of RNA degradation and abortive transcription initiation. Cells have specialized enzymes to degrade nanoRNAs, such as the DHH phosphoesterase family member NanoRNase A (NrnA). This enzyme was originally identified as a 3' → 5' exonuclease, but we show here that NrnA is bidirectional, degrading 2-5 nucleotide long RNA oligomers from the 3' end, and longer RNA substrates from the 5' end. The crystal structure of Bacillus subtilis NrnA reveals a dynamic bi-lobal architecture, with the catalytic N-terminal DHH domain linked to the substrate binding C-terminal DHHA1 domain via an extended linker. Whereas this arrangement is similar to the structure of RecJ, a 5' → 3' DHH family DNase and other DHH family nanoRNases, Bacillus NrnA has gained an extended substrate-binding patch that we posit is responsible for its 3' → 5' activity.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Schmier BJ,Nelersa CM,Malhotra A

doi

10.1038/s41598-017-09403-x

subject

Has Abstract

pub_date

2017-09-11 00:00:00

pages

11085

issue

1

issn

2045-2322

pii

10.1038/s41598-017-09403-x

journal_volume

7

pub_type

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