Monomeric YoeB toxin retains RNase activity but adopts an obligate dimeric form for thermal stability

Pavelich, Ian J.; Maehigashi, Tatsuya; Hoffer, Eric D.; Ruangprasert, Ajchareeya; Miles, Stacey J.; Dunham, Christine M.

doi:10.1093/nar/gkz760

Monomeric YoeB toxin retains RNase activity but adopts an obligate dimeric form for thermal stability

Journal Article · Tue Sep 10 00:00:00 EDT 2019 · Nucleic Acids Research

DOI:https://doi.org/10.1093/nar/gkz760· OSTI ID:1573380

Pavelich, Ian J. ^[1]; Maehigashi, Tatsuya ^[1]; Hoffer, Eric D. ^[1]; Ruangprasert, Ajchareeya ^[1]; Miles, Stacey J. ^[1]; Dunham, Christine M. ^[1]

Emory Univ. School of Medicine, Atlanta, GA (United States)

Chromosomally-encoded toxin-antitoxin complexes are ubiquitous in bacteria and regulate growth through the release of the toxin component typically in a stress-dependent manner. Type II ribosome-dependent toxins adopt a RelE-family RNase fold and inhibit translation by degrading mRNAs while bound to the ribosome. Here, we present biochemical and structural studies of the Escherichia coli YoeB toxin interacting with both a UAA stop and an AAU sense codon in pre- and post-mRNA cleavage states to provide insights into possible mRNA substrate selection. Both mRNAs undergo minimal changes during the cleavage event in contrast to type II ribosome-dependent RelE toxin. Further, the 16S rRNA decoding site nucleotides that monitor the mRNA in the aminoacyl(A) site adopt different orientations depending upon which toxin is present. Although YoeB is a RelE family member, it is the sole ribosome-dependent toxin that is dimeric. We show that engineered monomeric YoeB is active against mRNAs bound to both the small and large subunit. However, the stability of monomeric YoeB is reduced ~20°C, consistent with potential YoeB activation during heat shock in E. coli as previously demonstrated. These data provide a molecular basis for the ability of YoeB to function in response to thermal stress.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: USDOE Office of Science (SC); National Institutes of Health (NIH)

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1573380

Journal Information:: Nucleic Acids Research, Journal Name: Nucleic Acids Research Journal Issue: 19 Vol. 47; ISSN 0305-1048

Publisher:: Oxford University PressCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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