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Nat Rev Microbiol. 2013 Aug;11(8):525-38. doi: 10.1038/nrmicro3067. Epub 2013 Jul 8.

Breaking and joining single-stranded DNA: the HUH endonuclease superfamily.

Author information

1
Laboratoire de Microbiologie et Génétique Moléculaires, Centre National de la Recherche Scientifique, Toulouse Cedex, France. Michael.Chandler@ ibcg.biotoul.fr

Abstract

HUH endonucleases are numerous and widespread in all three domains of life. The major function of these enzymes is processing a range of mobile genetic elements by catalysing cleavage and rejoining of single-stranded DNA using an active-site Tyr residue to make a transient 5'-phosphotyrosine bond with the DNA substrate. These enzymes have a key role in rolling-circle replication of plasmids and bacteriophages, in plasmid transfer, in the replication of several eukaryotic viruses and in various types of transposition. They have also been appropriated for cellular processes such as intron homing and the processing of bacterial repeated extragenic palindromes. Here, we provide an overview of these fascinating enzymes and their functions, using well-characterized examples of Rep proteins, relaxases and transposases, and we explore the molecular mechanisms used in their diverse activities.

PMID:
23832240
PMCID:
PMC6493337
DOI:
10.1038/nrmicro3067
[Indexed for MEDLINE]
Free PMC Article

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