The structure of the KlcA and ArdB proteins reveals a novel fold and antirestriction activity against Type I DNA restriction systems in vivo but not in vitro
| Autor: | Gareth A. Roberts, John H. White, Garry W. Blakely, David T. F. Dryden, Dušan Uhrín, Andrew P. Herbert, Dinesh C. Soares, Dimitra Serfiotis-Mitsa |
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| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
Models
Molecular Transposable element Protein Folding Site-Specific DNA-Methyltransferase (Adenine-Specific) Molecular Sequence Data Biology medicine.disease_cause Bordetella pertussis 03 medical and health sciences chemistry.chemical_compound Plasmid Bacterial Proteins Structural Biology Escherichia coli Genetics medicine Amino Acid Sequence Nuclear Magnetic Resonance Biomolecular Peptide sequence Gene 030304 developmental biology 0303 health sciences Sequence Homology Amino Acid 030306 microbiology Escherichia coli Proteins Deoxyribonucleases Type I Site-Specific DNA Restriction Enzymes Endopeptidase Clp Pathogenicity island chemistry Biochemistry Mobile genetic elements Hydrophobic and Hydrophilic Interactions DNA |
| Zdroj: | Serfiotis-Mitsa, D, Herbert, A P, Roberts, G A, Soares, D C, White, J H, Blakely, G W, Uhrin, D & Dryden, D T F 2010, ' The structure of the KlcA and ArdB proteins reveals a novel fold and antirestriction activity against Type I DNA restriction systems in vivo but not in vitro ', Nucleic Acids Research, vol. 38, no. 5, pp. 1723-1737 . https://doi.org/10.1093/nar/gkp1144 Nucleic Acids Research |
| Popis: | Plasmids, conjugative transposons and phage frequently encode anti-restriction proteins to enhance their chances of entering a new bacterial host that is highly likely to contain a Type I DNA restriction and modification (RM) system. The RM system usually destroys the invading DNA. Some of the anti-restriction proteins are DNA mimics and bind to the RM enzyme to prevent it binding to DNA. In this article, we characterize ArdB anti-restriction proteins and their close homologues, the KlcA proteins from a range of mobile genetic elements; including an ArdB encoded on a pathogenicity island from uropathogenic Escherichia coli and a KlcA from an IncP-1b plasmid, pBP136 isolated from Bordetella pertussis. We show that all the ArdB and KlcA act as anti-restriction proteins and inhibit the four main families of Type I RM systems in vivo, but fail to block the restriction endonuclease activity of the archetypal Type I RM enzyme, EcoKI, in vitro indicating that the action of ArdB is indirect and very different from that of the DNA mimics. We also present the structure determined by NMR spectroscopy of the pBP136 KlcA protein. The structure shows a novel protein fold and it is clearly not a DNA structural mimic. |
| Databáze: | OpenAIRE |
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