Willkomm, Sarah and Makarova, Kira S. and Grohmann, Dina (2018) DNA silencing by prokaryotic Argonaute proteins adds a new layer of defense against invading nucleic acids. FEMS MICROBIOLOGY REVIEWS, 42 (3). pp. 376-387. ISSN 0168-6445, 1574-6976
Full text not available from this repository. (Request a copy)Abstract
Argonaute (Ago) proteins are encoded in all three domains of life and are responsible for the regulation of intracellular nucleic acid levels. Whereas some Ago variants are able to cleave target nucleic acids by their endonucleolytic activity, others only bind to their target nucleic acids while target cleavage is mediated by other effector proteins. Although all Ago proteins show a high degree of overall structural homology, the nature of the nucleic acid binding partners differs significantly. Recent structural and functional data have provided intriguing new insights into the mechanisms of archaeal and bacterial Ago variants demonstrating the mechanistic diversity within the prokaryotic Ago family with astonishing differences in nucleic acid selection and nuclease specificity. In this review, we provide an overview of the structural organisation of archaeal Ago variants and discuss the current understanding of their biological functions that differ significantly from their eukaryotic counterparts.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | GUIDE-RNA; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; BACTERIAL ARGONAUTE; COMPARATIVE GENOMICS; SLICER ACTIVITY; PIWI PROTEIN; INTERFERENCE; RECOGNITION; INSIGHTS; Argonaute; DNA-guided DNA silencing; antiviral defense; archaea; bacteria; prokaryotic Argonaute |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) > Prof. Dr. Dina Grohmann |
| Depositing User: | Petra Gürster |
| Date Deposited: | 30 Jun 2020 12:41 |
| Last Modified: | 30 Jun 2020 12:41 |
| URI: | https://pred.uni-regensburg.de/id/eprint/14620 |
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