Growth-regulating Mycobacterium tuberculosis VapC-mt4 toxin is an isoacceptor-specific tRNase

Jonathan W. Cruz, Jared D. Sharp, Eric D. Hoffer, Tatsuya Maehigashi, Irina O. Vvedenskaya, Arvind Konkimalla, Robert N. Husson, Bryce E. Nickels, Christine M. Dunham and Nancy A. Woychik ()
Additional contact information
Jonathan W. Cruz: Rutgers Robert Wood Johnson Medical School
Jared D. Sharp: Boston Children’s Hospital and Harvard Medical School
Eric D. Hoffer: Emory University School of Medicine
Tatsuya Maehigashi: Emory University School of Medicine
Irina O. Vvedenskaya: Waksman Institute, Rutgers University
Arvind Konkimalla: Rutgers Robert Wood Johnson Medical School
Robert N. Husson: Boston Children’s Hospital and Harvard Medical School
Bryce E. Nickels: Waksman Institute, Rutgers University
Christine M. Dunham: Emory University School of Medicine
Nancy A. Woychik: Rutgers Robert Wood Johnson Medical School

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: Abstract Toxin–antitoxin (TA) systems are implicated in the downregulation of bacterial cell growth associated with stress survival and latent tuberculosis infection, yet the activities and intracellular targets of these TA toxins are largely uncharacterized. Here, we use a specialized RNA-seq approach to identify targets of a Mycobacterium tuberculosis VapC TA toxin, VapC-mt4 (also known as VapC4), which have eluded detection using conventional approaches. Distinct from the one other characterized VapC toxin in M. tuberculosis that cuts 23S rRNA at the sarcin–ricin loop, VapC-mt4 selectively targets three of the 45 M. tuberculosis tRNAs (tRNAAla2, tRNASer26 and tRNASer24) for cleavage at, or adjacent to, their anticodons, resulting in the generation of tRNA halves. While tRNA cleavage is sometimes enlisted as a bacterial host defense mechanism, VapC-mt4 instead alters specific tRNAs to inhibit translation and modulate growth. This stress-linked activity of VapC-mt4 mirrors basic features of eukaryotic tRNases that also generate tRNA halves and inhibit translation in response to stress.

Date: 2015
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms8480 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8480

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms8480

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().