Breaking and joining single-stranded DNA: the HUH endonuclease superfamily View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2013-08

AUTHORS

Michael Chandler, Fernando de la Cruz, Fred Dyda, Alison B. Hickman, Gabriel Moncalian, Bao Ton-Hoang

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. More... »

PAGES

525

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nrmicro3067

DOI

http://dx.doi.org/10.1038/nrmicro3067

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1014381933

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/23832240


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