Journal
NUCLEIC ACIDS RESEARCH
Volume 39, Issue 17, Pages 7620-7629Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkr397
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Funding
- Natural Sciences and Engineering Research Council (NSERC) of Canada [03601-CG083160]
- Alberta Heritage Foundation for Medical Research
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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.
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