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Nucleic Acids Research Advance Access first published online on August 30, 2007
This version published online on September 6, 2007
Nucleic Acids Research, doi:10.1093/nar/gkm554
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© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

An archaeal orthologue of the universal protein Kae1 is an iron metalloprotein which exhibits atypical DNA-binding properties and apurinic-endonuclease activity in vitro

Arnaud Hecker1, Nicolas Leulliot2, Danièle Gadelle1, Marc Graille2, Anthony Justome3, Pierre Dorlet4, Céline Brochier5,6, Sophie Quevillon-Cheruel2, Eric Le Cam3, Herman van Tilbeurgh2 and Patrick Forterre1,7,*

1Institut de Génétique et Microbiologie, Univ. Paris-Sud, IFR115, UMR8621-CNRS, 91405 Orsay, France, 2Institut de Biochimie et de Biophysique Moléculaire et Cellulaire, Univ. Paris-Sud, IFR115, UMR8619-CNRS, 91405 Orsay, France, 3Institut Gustave Roussy, Interactions Moléculaires et Cancer, UMR8126-CNRS, 94805 Villejuif Cedex, France, 4Institut de Chimie Moléculaire et des Matériaux, Univ. Paris-Sud, UMR8182-CNRS, 91405 Orsay, France, 5Institut de Biologie Structurale et de Microbiologie, Laboratoire de Chimie Bactérienne, UPR9043-CNRS, 13402 Marseille Cedex 20, France, 6Université de Provence - Aix-Marseille I, 13331 Marseille Cedex 3, France and 7Institut Pasteur, Unité Biologie Moléculaire du Gène chez les Extrêmophiles, 25 rue du Dr Roux, 75724 Paris Cedex 15, France

*To whom correspondence should be addressed. Tel: +33 1 69 15 74 89; Fax: +33 1 69 15 78 08; Email: patrick.forterre{at}igmors.u-psud.fr Correspondence may also be addressed to Herman van Tilbeurgh. Email: herman.van-tilbeurgh{at}u-psud.fr

Received April 25, 2007. Revised July 3, 2007. Accepted July 5, 2007.

The Kae1 (Kinase-associated endopeptidase 1) protein is a member of the recently identified transcription complex EKC and telomeres maintenance complex KEOPS in yeast. Kae1 homologues are encoded by all sequenced genomes in the three domains of life. Although annotated as putative endopeptidases, the actual functions of these universal proteins are unknown. Here we show that the purified Kae1 protein (Pa-Kae1) from Pyrococcus abyssi is an iron-protein with a novel type of ATP-binding site. Surprisingly, this protein did not exhibit endopeptidase activity in vitro but binds cooperatively to single and double-stranded DNA and induces unusual DNA conformational change. Furthermore, Pa-Kae1 exhibits a class I apurinic (AP)-endonuclease activity (AP-lyase). Both DNA binding and AP-endonuclease activity are inhibited by ATP. Kae1 is thus a novel and atypical universal DNA interacting protein whose importance could rival those of RecA (RadA/Rad51) in the maintenance of genome integrity in all living cells.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.


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