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Structure-functiona...
Structure-functional characterization of Lactococcus AbiA phage defense system
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- Gapińska, Marta (author)
- International Institute of Molecular and Cell Biology, Warsaw
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- Zajko, Weronika (author)
- International Institute of Molecular and Cell Biology, Warsaw
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- Skowronek, Krzysztof (author)
- International Institute of Molecular and Cell Biology, Warsaw
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- Figiel, Małgorzata (author)
- International Institute of Molecular and Cell Biology, Warsaw
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- Krawczyk, Paweł S (author)
- International Institute of Molecular and Cell Biology, Warsaw
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- Egorov, Artyom A (author)
- Lund University,Lunds universitet,Institutionen för experimentell medicinsk vetenskap,Medicinska fakulteten,Proteinevolution,Forskargrupper vid Lunds universitet,Department of Experimental Medical Science,Faculty of Medicine,Protein Evolution,Lund University Research Groups
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- Dziembowski, Andrzej (author)
- International Institute of Molecular and Cell Biology, Warsaw
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- Johansson, Marcus J O (author)
- Lund University,Lunds universitet,Institutionen för experimentell medicinsk vetenskap,Medicinska fakulteten,Molekylär enzymologi,Forskargrupper vid Lunds universitet,Department of Experimental Medical Science,Faculty of Medicine,Molecular Enzymology,Lund University Research Groups
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- Nowotny, Marcin (author)
- International Institute of Molecular and Cell Biology, Warsaw
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(creator_code:org_t)
- 2024
- 2024
- English 16 s.
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In: Nucleic Acids Research. - 1362-4962. ; 52:8, s. 4723-4738
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Abstract
Subject headings
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- Bacterial reverse transcriptases (RTs) are a large and diverse enzyme family. AbiA, AbiK and Abi-P2 are abortive infection system (Abi) RTs that mediate defense against bacteriophages. What sets Abi RTs apart from other RT enzymes is their ability to synthesize long DNA products of random sequences in a template- and primer-independent manner. Structures of AbiK and Abi-P2 representatives have recently been determined, but there are no structural data available for AbiA. Here, we report the crystal structure of Lactococcus AbiA polymerase in complex with a single-stranded polymerization product. AbiA comprises three domains: an RT-like domain, a helical domain that is typical for Abi polymerases, and a higher eukaryotes and prokaryotes nucleotide-binding (HEPN) domain that is common for many antiviral proteins. AbiA forms a dimer that distinguishes it from AbiK and Abi-P2, which form trimers/hexamers. We show the DNA polymerase activity of AbiA in an in vitro assay and demonstrate that it requires the presence of the HEPN domain which is enzymatically inactive. We validate our biochemical and structural results in vivo through bacteriophage infection assays. Finally, our in vivo results suggest that AbiA-mediated phage defense may not rely on AbiA-mediated cell death.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Microbiology in the medical area (hsv//eng)
Keyword
- Bacteriophages/genetics
- Lactococcus/virology
- Models, Molecular
- Bacterial Proteins/metabolism
- Crystallography, X-Ray
- Protein Domains
- RNA-Directed DNA Polymerase/metabolism
- Protein Multimerization
- Structure-Activity Relationship
Publication and Content Type
- art (subject category)
- ref (subject category)
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