The archaeal RecJ-like proteins : nucleases and ex-nucleases with diverse roles in replication and repair
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RecJ proteins belong to the DHH superfamily of phosphoesterases that has members in all three domains of life. In bacteria, the archetypal RecJ is a 5’→3’ ssDNA exonuclease that functions in homologous recombination, base excision repair and mismatch repair, while in eukaryotes, the RecJ-like protein Cdc45 (which has lost its nuclease activity) is a key component of the CMG (Cdc45-MCM-GINS) complex, the replicative DNA helicase that unwinds double-stranded DNA at the replication fork. In archaea, database searching identifies genes encoding one or more RecJ family proteins in almost all sequenced genomes. Biochemical analysis has confirmed that some but not all of these proteins are components of archaeal CMG complexes and has revealed a surprising diversity in mode of action and substrate preference. In addition to this, some archaea encode catalytically inactive RecJ-like proteins, and others a mix of active and inactive proteins, with the inactive proteins being confined to structural roles only. Here, I summarise current knowledge of the structure and function of the archaeal RecJ-like proteins, focusing on similarities and differences between proteins from different archaeal species, between proteins within species, and between the archaeal proteins and their bacterial and eukaryotic relatives. Models for RecJ-like function are described and key areas for further study highlighted.
MacNeill , S A 2018 , ' The archaeal RecJ-like proteins : nucleases and ex-nucleases with diverse roles in replication and repair ' , Emerging Topics in Life Sciences , vol. 2 , no. 4 , pp. 493-501 . https://doi.org/10.1042/ETLS20180017
Emerging Topics in Life Sciences
© 2018, The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society and the Royal Society of Biology. This work has been made available online in accordance with the publisher’s policies. This is the author created accepted version manuscript following peer review and as such may differ slightly from the final published version. The final published version of this work is available at https://doi.org/10.1042/ETLS20180017
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