tRNA anticodon cleavage by target-activated CRISPR-Cas13a effector

Author:

Jain Ishita1ORCID,Kolesnik Matvey2ORCID,Kuznedelov Konstantin1ORCID,Minakhin Leonid1,Morozova Natalia3ORCID,Shiriaeva Anna34ORCID,Kirillov Alexandr3,Medvedeva Sofia2,Livenskyi Alexei56ORCID,Kazieva Laura7ORCID,Makarova Kira S.8ORCID,Koonin Eugene V.8ORCID,Borukhov Sergei9ORCID,Severinov Konstantin15ORCID,Semenova Ekaterina1ORCID

Affiliation:

1. Waksman Institute for Microbiology, Rutgers, The State University of New Jersey, Piscataway, NJ, USA.

2. Center for Molecular and Cellular Biology, Skolkovo Institute of Science and Technology, Moscow, Russia.

3. Peter the Great St. Petersburg Polytechnic University, Saint Petersburg, Russia.

4. Saint Petersburg State University, Saint Petersburg, Russia.

5. Center for Precision Genome Editing and Genetic Technologies for Biomedicine, Institute of Gene Biology, Moscow, Russia.

6. Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russia.

7. Institute of Biomedical Chemistry, Moscow, Russia.

8. National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health; Bethesda, MD, USA.

9. Department of Cell Biology and Neuroscience, Rowan University School of Osteopathic Medicine at Stratford; Stratford, NJ, USA.

Abstract

Type VI CRISPR-Cas systems are among the few CRISPR varieties that target exclusively RNA. The CRISPR RNA–guided, sequence-specific binding of target RNAs, such as phage transcripts, activates the type VI effector, Cas13. Once activated, Cas13 causes collateral RNA cleavage, which induces bacterial cell dormancy, thus protecting the host population from the phage spread. We show here that the principal form of collateral RNA degradation elicited by Leptotrichia shahii Cas13a expressed in Escherichia coli cells is the cleavage of anticodons in a subset of transfer RNAs (tRNAs) with uridine-rich anticodons. This tRNA cleavage is accompanied by inhibition of protein synthesis, thus providing defense from the phages. In addition, Cas13a-mediated tRNA cleavage indirectly activates the RNases of bacterial toxin-antitoxin modules cleaving messenger RNA, which could provide a backup defense. The mechanism of Cas13a-induced antiphage defense resembles that of bacterial anticodon nucleases, which is compatible with the hypothesis that type VI effectors evolved from an abortive infection module encompassing an anticodon nuclease.

Publisher

American Association for the Advancement of Science (AAAS)

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