A reverse transcriptase-related protein mediates phage resistance and polymerizes untemplated DNA in vitro
| Autor: | Sylvain Moineau, Manuela Villion, Cameron Semper, Colin Coros, Chen Wang, Steven Zimmerly |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
DNA polymerase
Amino Acid Motifs Molecular Sequence Data Retrotransposon DNA-Directed DNA Polymerase 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Genetics Bacteriophages Amino Acid Sequence Peptide sequence Polymerase 030304 developmental biology 0303 health sciences biology Sequence Homology Amino Acid 030306 microbiology Nucleic Acid Enzymes RNA-Directed DNA Polymerase DNA Molecular biology Reverse transcriptase Protein Structure Tertiary Lactococcus lactis Biochemistry chemistry Mutation biology.protein Primer (molecular biology) |
| Zdroj: | Nucleic Acids Research |
| ISSN: | 1362-4962 0305-1048 |
| Popis: | Reverse transcriptases (RTs) are RNA-dependent DNA polymerases that usually function in the replication of selfish DNAs such as retrotransposons and retroviruses. Here, we have biochemically characterized a RT-related protein, AbiK, which is required for abortive phage infection in the Gram-positive bacterium Lactococcus lactis. In vitro, AbiK does not exhibit the properties expected for an RT, but polymerizes long DNAs of 'random' sequence, analogous to a terminal transferase. Moreover, the polymerized DNAs appear to be covalently attached to the AbiK protein, presumably because an amino acid serves as a primer. Mutagenesis experiments indicate that the polymerase activity resides in the RT motifs and is essential for phage resistance in vivo. These results establish a novel biochemical property and a non-replicative biological role for a polymerase. |
| Databáze: | OpenAIRE |
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